TY - JOUR AU - McCann, Sinead AU - Roe, William E. AU - Agnew, Hannah E. AU - Knipe, Peter C. TI - Non-Covalent Interactions Enforce Conformation in Switchable and Water-Soluble Diketopiperazine-Pyridine Foldamers JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 62 PY - 2023 IS - 35 PG - 5 SN - 1433-7851 DO - 10.1002/anie.202307180 UR - https://m2.mtmt.hu/api/publication/34294004 ID - 34294004 AB - To reach their potential as mimics of the dynamic molecules present in biological systems, foldamers must be designed to display stimulus-responsive behavior. Here we report such a foldamer architecture based on alternating pyridine-diketopiperazine linkers. Epimerization is conveniently prevented through a copper-catalyzed coupling protocol. The compounds' native unswitched conformation is first discovered in the solid and solution state. The foldamers can be solubilized in DMSO and pH 9.5 buffer, retaining conformational control to a large degree. Lastly, dynamic switching is demonstrated through treatment with acid, leading to behaviour we describe as stimulus-responsive sidechain reconfiguration. LA - English DB - MTMT ER - TY - JOUR AU - Patel, Mohit B. AU - Spikes, Helena AU - Bailey, Robert S. AU - Connell, Thomas AU - Gill, Hannah AU - Gokel, Michael R. AU - Harris, Rebecca AU - Meisel, Joseph W. AU - Negin, Saeedeh AU - Yin, Shanheng Andrew AU - Gokel, George W. TI - Antimicrobial and Adjuvant Potencies of Di-n-alkyl Substituted Diazalariat Ethers JF - ANTIBIOTICS J2 - ANTIBIOTICS-BASEL VL - 12 PY - 2023 IS - 10 PG - 23 SN - 2079-6382 DO - 10.3390/antibiotics12101513 UR - https://m2.mtmt.hu/api/publication/34616533 ID - 34616533 AB - Lariat ethers are macrocyclic polyethers-crown ethers-to which sidearms are appended. 4,13-Diaza-18-crown-6 having twin alkyl chains at the nitrogens show biological activity. They exhibit antibiotic activity, but when co-administered at with an FDA-approved antibiotic, the latter's potency is often strongly enhanced. Potency enhancements and resistance reversals have been documented in vitro for a range of Gram-negative and Gram-positive bacteria with a variety of antimicrobials. Strains of E. coli and Staphylococcus aureus having resistance to a range of drugs have been studied and the potency enhancements (checkerboards) are reported here. Drugs included in the present study are ampicillin, cefepime, chlortetracycline, ciprofloxacin, doxycycline, kanamycin, minocycline, norfloxacin, oxycycline, penicillin G, and tetracycline. Enhancements of norfloxacin potency against S. aureus 1199B of up to 128-fold were observed. The properties of these lariat ethers have been studied to determine solubility, their membrane penetration, cytotoxicity and mammalian cell survival, and their effect on bacterial efflux pumps. It is shown that in some cases, the lariat ethers have complex antimicrobials with considerable selectivity. Based on these observations, including 1:1 complexation between lariat ethers and antimicrobials and the cytotoxicity of the MeI salts showing a separation index of 32-fold, they hold significant potential for further development. LA - English DB - MTMT ER - TY - JOUR AU - Shen, Aizong AU - Zhang, Lei AU - Xie, Yanbo AU - Zhu, Xueyu AU - Hu, Jinming AU - Liu, Shiyong TI - Engineering discrete synthetic macromolecules for biomedical applications JF - NANO TODAY J2 - NANO TODAY VL - 48 PY - 2023 PG - 15 SN - 1748-0132 DO - 10.1016/j.nantod.2022.101728 UR - https://m2.mtmt.hu/api/publication/33903404 ID - 33903404 AB - Synthetic polymers have been extensively used in biomedical fields for imaging and therapeutic purposes. These macromolecular nanomedicines have shown unique advantages, such as increased blood circulation time, decreased systemic toxicity, and improved therapeutic outcomes. However, the polydisperse mole-cular weight of conventional polymers greatly hampers the reproducibility and clinical translations of macromolecular nanomedicines. Unlike conventional polymers with molecular weight distributions, dis-crete polymers are characterized by precise molecular weight and no molecular weight distribution (D = 1.0). Although discrete polymers have similar chemical structures and compositions to those of their dis-perse counterparts, they can show drastically distinct physiochemical properties and thus different bio-medical performance. In this review, we summarize the recent achievements of discrete polymers in optical imaging, magnetic resonance (MR) imaging, and therapeutic applications. In addition, the representative methods used to synthesize discrete polymers are briefly discussed. Although this field represents an emerging research direction, preliminary results are encouraging and promising in many aspects. Due to the structural similarity of discrete and disperse polymers, their precise structures and improved performance may greatly facilitate their clinical translation into precision nanomedicines. We hope that more effort will be devoted to the development of highly efficient synthetic strategies and the conduction of (pre)clinical studies of discrete polymers. An in-depth understanding of the structure-property relationships of discrete polymers can be advantageous to boost their practical applications. (c) 2022 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Shi, Chenghui AU - Kaffy, Julia AU - Ha-Duong, Tap AU - Gallard, Jean-Francois AU - Pruvost, Alain AU - Mabondzo, Aloise AU - Ciccone, Lidia AU - Ongeri, Sandrine AU - Tonali, Nicolo TI - Proteolytically Stable Diaza-Peptide Foldamers Mimic Helical Hot Spots of Protein-Protein Interactions and Act as Natural Chaperones JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 66 PY - 2023 IS - 17 SP - 12005 EP - 12017 PG - 13 SN - 0022-2623 DO - 10.1021/acs.jmedchem.3c00611 UR - https://m2.mtmt.hu/api/publication/34294003 ID - 34294003 AB - A novel class of peptidomimetic foldamers based on diaza-peptide units are reported. Circular dichroism, attenuated total reflection -Fourier transform infrared, NMR, and molecular dynamics studies demonstrate that unlike the natural parent nonapeptide, the specific incorporation of one diaza-peptide unit at the N-terminus allows helical folding in water, which is further reinforced by the introduction of a second unit at the C-terminus. The ability of these foldamers to resist proteolysis, to mimic the small helical hot spot of transthyretin-amyloid ss (A ss) cross-interaction, and to decrease pathological A ss aggregation demonstrates that the introduction of diaza-peptide units is a valid approach for designing mimics or inhibitors of protein-protein interaction and other therapeutic peptidomimetics. This study also reveals that small peptide foldamers can play the same role as physiological chaperone proteins and opens a new way to design inhibitors of amyloid protein aggregation, a hallmark of more than 20 serious human diseases such as Alzheimer's disease. LA - English DB - MTMT ER - TY - JOUR AU - Wacha, András Ferenc AU - Varga, Zoltán AU - Beke-Somfai, Tamás TI - Comparative Study of Molecular Mechanics Force Fields for β-Peptidic Foldamers: Folding and Self-Association JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 63 PY - 2023 IS - 12 SP - 3799 EP - 3813 PG - 15 SN - 1549-9596 DO - 10.1021/acs.jcim.3c00175 UR - https://m2.mtmt.hu/api/publication/34044318 ID - 34044318 LA - English DB - MTMT ER - TY - JOUR AU - Bodero, L. AU - Guitot, K. AU - Lensen, N. AU - Lequin, O. AU - Brigaud, T. AU - Ongeri, S. AU - Chaume, G. TI - Introducing the Chiral Constrained α-Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw-Sense** JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 28 PY - 2022 IS - 8 SN - 0947-6539 DO - 10.1002/chem.202103887 UR - https://m2.mtmt.hu/api/publication/32695477 ID - 32695477 N1 - CY Cergy Paris Université, CNRS, BioCIS, Cergy Pontoise, 95000, France Université Paris-Saclay, CNRS, BioCIS, Châtenay-Malabry, 92290, France Sorbonne Université, École Normale Supérieure, PSL University, CNRS, Laboratoire des Biomolécules, LBM, Paris, 75005, France Export Date: 21 February 2022 CODEN: CEUJE Correspondence Address: Chaume, G.; CY Cergy Paris Université, France; email: gregory.chaume@cyu.fr Correspondence Address: Ongeri, S.; Université Paris-Saclay, France; email: sandrine.ongeri@universite-paris-saclay.fr Chemicals/CAS: alanine, 56-41-7, 6898-94-8; Alanine; alpha-trifluoromethylalanine Funding details: CNRS-UPR2301 Funding text 1: The CY Initiative of Excellence (grant ?Investissements d?Avenir? INEX 2019 FluoSPep) is thanked for financial support of Lizeth Bodero. Authors thank Dr. Pascal Retailleau (Departement of X-ray crystallography at Institut de Chimie des Substances Naturelles ? UPS, CNRS-UPR2301 ? Gif sur Yvette) for help with the crystal structure solution. Funding text 2: The CY Initiative of Excellence (grant “Investissements d′Avenir” INEX 2019 FluoSPep) is thanked for financial support of Lizeth Bodero. Authors thank Dr. Pascal Retailleau (Departement of X‐ray crystallography at Institut de Chimie des Substances Naturelles – UPS, CNRS‐UPR2301 – Gif sur Yvette) for help with the crystal structure solution. AB - Oligomers of α-aminoisobutyric acid (Aib) are achiral peptides that adopt 310 helical structures with equal population of left- and right-handed conformers. The screw-sense preference of the helical chain may be controlled by a single chiral residue located at one terminus. 1H and 19F NMR, X-ray crystallography and circular dichroism studies on new Aib oligomers show that the incorporation of a chiral quaternary α-trifluoromethylalanine at their N-terminus induces a reversal of the screw-sense preference of the 310-helix compared to that of a non-fluorinated analogue having an l-α-methyl valine residue. This work demonstrates that, among the many particular properties of introducing a trifluoromethyl group into foldamers, its stereo-electronic properties are of major interest to control the helical screw sense. Its use as an easy-to-handle 19F NMR probe to reliably determine both the magnitude of the screw-sense preference and its sign assignment is also of remarkable interest. © 2021 Wiley-VCH GmbH. LA - English DB - MTMT ER - TY - JOUR AU - Giuffrida, S.G. AU - Forysiak, W. AU - Cwynar, P. AU - Szweda, R. TI - Shaping Macromolecules for Sensing Applications—From Polymer Hydrogels to Foldamers JF - POLYMERS J2 - POLYMERS-BASEL VL - 14 PY - 2022 IS - 3 PG - 32 SN - 2073-4360 DO - 10.3390/polym14030580 UR - https://m2.mtmt.hu/api/publication/32695478 ID - 32695478 AB - Sensors are tools for detecting, recognizing, and recording signals from the surrounding environment. They provide measurable information on chemical or physical changes, and thus are widely used in diagnosis, environment monitoring, food quality checks, or process control. Polymers are versatile materials that find a broad range of applications in sensory devices for the bio-medical sector and beyond. Sensory materials are expected to exhibit a measurable change of properties in the presence of an analyte or a stimulus, characterized by high sensitivity and selectivity of the signal. Signal parameters can be tuned by material features connected with the restriction of macromolecule shape by crosslinking or folding. Gels are crosslinked, three-dimensional networks that can form cavities of different sizes and forms, which can be adapted to trap particular analytes. A higher level of structural control can be achieved by foldamers, which are macromolecules that can attain well-defined conformation in solution. By increasing control over the three-dimensional structure, we can improve the selectivity of polymer materials, which is one of the crucial requirements for sensors. Here, we discuss various examples of polymer gels and foldamer-based sensor systems. We have classified and described applied polymer materials and used sensing techniques. Finally, we deliberated the necessity and potential of further exploration of the field towards the increased selectivity of sensory devices. © 2022 by the authors. Licensee MDPI, Basel, Switzerland. LA - English DB - MTMT ER - TY - JOUR AU - Shi, Chenghui AU - Correia, Isabelle AU - Tonali, Nicolo AU - Ongeri, Sandrine AU - Lequin, Olivier TI - Two consecutive aza-amino acids in peptides promote stable beta-turn formation in water JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 20 PY - 2022 IS - 43 SP - 8430 EP - 8437 PG - 9 SN - 1477-0520 DO - 10.1039/d2ob01225a UR - https://m2.mtmt.hu/api/publication/33305100 ID - 33305100 N1 - Université Paris-Saclay, CNRS, BioCIS, Châtenay-Malabry, 92290, France Sorbonne Université, Ecole Normale Supérieure, PSL University, CNRS, Laboratoire des Biomolécules, 4 place Jussieu, Paris, 75252 Cedex, France Export Date: 27 January 2023 CODEN: OBCRA Correspondence Address: Ongeri, S.; Université Paris-Saclay, France; email: sandrine.ongeri@universite-paris-saclay.fr Correspondence Address: Lequin, O.; Sorbonne Université, 4 place Jussieu, France; email: olivier.lequin@sorbonne-universite.fr AB - Studies on the synthetic methodologies and the structural propensity of peptides containing consecutive aza-amino acids are still in their infancy. Here, details of the synthesis and conformational analysis of tripeptides containing two consecutive aza-amino acids are provided. The demonstration that the type I beta-turn folding is induced, even in aqueous media, by the introduction of one or two lateral chains on the diaza-peptide unit is of particular importance for the design of peptidomimetics of biological interest. LA - English DB - MTMT ER - TY - JOUR AU - Takada, Hiroyuki AU - Tsuchiya, Keisuke AU - Demizu, Yosuke TI - Helix-Stabilized Cell-Penetrating Peptides for Delivery of Antisense Morpholino Oligomers: Relationships among Helicity, Cellular Uptake, and Antisense Activity JF - BIOCONJUGATE CHEMISTRY J2 - BIOCONJUGATE CHEM VL - 33 PY - 2022 IS - 7 SP - 1311 EP - 1318 PG - 8 SN - 1043-1802 DO - 10.1021/acs.bioconjchem.2c00199 UR - https://m2.mtmt.hu/api/publication/33305101 ID - 33305101 N1 - Division of Organic Chemistry, National Institute of Health Sciences, Kanagawa, 210-9501, Japan Graduate School of Medical Life Science, Yokohama City University, Kanagawa, 236-0027, Japan Graduate School of Pharmacy, Showa University, Tokyo, 142-8555, Japan Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, 700-8530, Japan Cited By :1 Export Date: 27 January 2023 CODEN: BCCHE Correspondence Address: Demizu, Y.; Division of Organic Chemistry, Japan; email: demizu@nihs.go.jp AB - The secondary structures of cell-penetrating peptides (CPPs) influence their properties including their cell membrane permeability, tolerability to proteases, and intracellular distribution. Herein, we developed helix-stabilized arginine-rich peptides containing alpha,alpha-disubstituted alpha-amino acids and their conjugates with antisense phosphorodiamidate morpholino oligomers (PMOs), to investigate the relationships among the helicity of the peptides, cellular uptake, and antisense activity of the peptide-conjugated PMOs. We demonstrated that helical CPPs can efficiently deliver the conjugated PMO into cells compared with nonhelical CPPs and that their antisense activities are synergistically enhanced in the presence of an endosomolytic reagent or an endosomal escape domain peptide. LA - English DB - MTMT ER - TY - JOUR AU - Tsuchiya, Keisuke AU - Kurohara, Takashi AU - Fukuhara, Kiyoshi AU - Misawa, Takashi AU - Demizu, Yosuke TI - Helical Foldamers and Stapled Peptides as New Modalities in Drug Discovery: Modulators of Protein-Protein Interactions JF - PROCESSES J2 - PROCESSES VL - 10 PY - 2022 IS - 5 PG - 24 SN - 2227-9717 DO - 10.3390/pr10050924 UR - https://m2.mtmt.hu/api/publication/33305102 ID - 33305102 N1 - Division of Organic Chemistry, National Institute of Health Sciences, 3-25-26, Tonomachi, Kanagawa, Kawasaki, 210-9501, Japan Graduate School of Pharmacy, Showa University, 1-5-8, Hatanodai, Shinagawa-ku, Tokyo, 142-0064, Japan Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Yokohama, Kanagawa230-0045, Japan Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, 1-1-1 Tsushima-naka, Kita-ku, Okayama, 700-8530, Japan Cited By :1 Export Date: 27 January 2023 Correspondence Address: Misawa, T.; Division of Organic Chemistry, 3-25-26, Tonomachi, Kanagawa, Japan; email: misawa@nihs.go.jp Correspondence Address: Demizu, Y.; Division of Organic Chemistry, 3-25-26, Tonomachi, Kanagawa, Japan; email: demizu@nihs.go.jp AB - A "foldamer" is an artificial oligomeric molecule with a regular secondary or tertiary structure consisting of various building blocks. A "stapled peptide" is a peptide with stabilized secondary structures, in particular, helical structures by intramolecular covalent side-chain cross-linking. Helical foldamers and stapled peptides are potential drug candidates that can target protein-protein interactions because they enable multipoint molecular recognition, which is difficult to achieve with low-molecular-weight compounds. This mini-review describes a variety of peptide-based foldamers and stapled peptides with a view to their applications in drug discovery, including our recent progress. LA - English DB - MTMT ER - TY - CHAP AU - Zorko, M. AU - Langel, Ü. ED - Sunil, Thomas TI - Cell-Penetrating Peptides T2 - Vaccine Design VL - 2383 PB - Humana Press CY - New York, New York SN - 9781071618912 T3 - Methods in Molecular Biology, ISSN 1064-3745 ; 2412. PY - 2022 SP - 3 EP - 32 PG - 30 DO - 10.1007/978-1-0716-1752-6_1 UR - https://m2.mtmt.hu/api/publication/32695479 ID - 32695479 N1 - Medical Faculty, Institute of Biochemistry and Molecular Genetics, University of Ljubljana, Ljubljana, Slovenia Department of Biochemistry and Biophysics, University of Stockholm, Stockholm, Sweden Institute of Technology, University of Tartu, Tartu, Estonia Export Date: 21 February 2022 Correspondence Address: Zorko, M.; Medical Faculty, Slovenia; email: zorko@mf.uni-lj.si Chemicals/CAS: carrier protein, 80700-39-6; Cell-Penetrating Peptides AB - In this introductory chapter, we first define cell-penetrating peptides (CPPs), give short overview of CPP history and discuss several aspects of CPP classification. Next section is devoted to the mechanism of CPP penetration into the cells, where direct and endocytic internalization of CPP is explained. Kinetics of internalization is discussed more extensively, since this topic is not discussed in other chapters of this book. At the end of this section some features of the thermodynamics of CPP interaction with the membrane is also presented. Finally, we present different cargoes that can be transferred into the cells by CPPs and briefly discuss the effect of cargo on the rate and efficiency of penetration into the cells. © 2022, The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature. LA - English DB - MTMT ER - TY - JOUR AU - Adaligil, Emel AU - Song, Aimin AU - Hallenbeck, Kenneth K. AU - Cunningham, Christian N. AU - Fairbrother, Wayne J. TI - Ribosomal Synthesis of Macrocyclic Peptides with beta(2)- and beta(2,3)-Homo-Amino Acids for the Development of Natural Product-Like Combinatorial Libraries JF - ACS CHEMICAL BIOLOGY J2 - ACS CHEM BIOL VL - 16 PY - 2021 IS - 6 SP - 1011 EP - 1018 PG - 8 SN - 1554-8929 DO - 10.1021/acschembio.1c00062 UR - https://m2.mtmt.hu/api/publication/32367953 ID - 32367953 N1 - Cited By :7 Export Date: 27 January 2023 CODEN: ACBCC Correspondence Address: Cunningham, C.N.; Department of Early Discovery Biochemistry, 1 DNA Way, United States; email: cunningham.christian@gene.com Correspondence Address: Fairbrother, W.J.; Department of Early Discovery Biochemistry, 1 DNA Way, United States; email: fairbrother.wayne@gene.com AB - The development of large, natural-product-like, combinatorial macrocyclic peptide libraries is essential in the quest to develop therapeutics for "undruggable" cellular targets. Herein we report the ribosomal synthesis of macrocyclic peptides containing one or more beta(2)-homo-amino acids (beta(2)haa) to enable their incorporation into mRNA display-based selection libraries. We confirmed the compatibility of 14 beta(2)-homo-amino acids, (S)- and (R)-stereochemistry, for single incorporation into a macrocyclic peptide with low to high translation efficiency. Interestingly, N-methylation of the backbone amide of beta(2)haa prevented the incorporation of this amino acid subclass by the ribosome. Additionally, we designed and incorporated several alpha,beta-disubstituted beta(2,3)-homo-amino acids (beta(2,3)haa) with different R-groups on the alpha- and beta-carbons of the same amino acid. Incorporation of these beta(2,3)haa enables increased diversity in a single position of a macrocyclic peptide without significantly increasing the overall molecular weight, which is an important consideration for passive cell permeability. We also successfully incorporated multiple (S)-beta(2)hAla into a single macrocycle with other non-proteinogenic amino acids, confirming that this class of beta-amino acid is suitable for development of large scale macrocyclic peptide libraries. LA - English DB - MTMT ER - TY - JOUR AU - Laxio Arenas, Jose AU - Xu, Yaochun AU - Milcent, Thierry AU - Van Heijenoort, Carine AU - Giraud, Francois AU - Ha-Duong, Tap AU - Crousse, Benoit AU - Ongeri, Sandrine TI - Fluorinated Triazole Foldamers: Folded or Extended Conformational Preferences JF - CHEMPLUSCHEM J2 - CHEMPLUSCHEM VL - 86 PY - 2021 IS - 2 SP - 241 EP - 251 PG - 11 SN - 2192-6506 DO - 10.1002/cplu.202000791 UR - https://m2.mtmt.hu/api/publication/32370554 ID - 32370554 N1 - BioCIS, CNRS, Université Paris Saclay, 5 rue Jean-baptiste Clément, Châtenay-Malabry Cedex, 92296, France Equipe Biologie et Chimie Structurales, Dept Chimie et Biologie Structurales et Analytiques, ICSN, CNRS, Université Paris Saclay, 1 avenue de la terrasse, Gif sur Yvette, 91190, France Cited By :1 Export Date: 21 February 2022 CODEN: CHEMM Correspondence Address: Ongeri, S.; BioCIS, 5 rue Jean-baptiste Clément, France; email: sandrine.ongeri@universite-paris-saclay.fr Funding details: Ministère de l'Enseignement Supérieur et de la Recherche, MESR Funding text 1: The Ministère de l'Enseignement Supérieur et de la Recherche (MESR) is thanked for financial support for José Laxio Arenas. The China Scholarship Council is thanked for financial support for Yaochun Xu. The authors thank Pr. Vadim Soloshonok and TOSOH F‐TECH, Inc. for the kind gift of N‐terbutyl‐sulfinylimine. AB - Fluorinated peptidomimetic foldamers are still in their infancy. We report here the easy access to fluorinated triazolamers based on 2-amino-3,3,3-trifluoropropyl-1,4-triazolyl acetic acid (CF3-1,4-Tz) and on aminomethyl-1,4-triazolyl-difluoroacetic acid (1,4-Tz-CF2). Both CF3-1,4-Tz and 1,4-Tz-CF2 amino acids were efficiently prepared by copper(I)-catalyzed Huisgen 1,3-dipolar cycloaddition. Their conformational preferences were studied by 2D NMR analyses and molecular dynamic simulations. Foldamers based on CF3-1,4-Tz amino acids are capable of adopting short multi-stranded beta-sheet-like structures that are maintained by electrostatic interactions between the triazole proton and N2 atom of neighboring subunits. On the contrary, foldamers based on 1,4-Tz-CF2 units adopt elongated beta-strand-like structures, stabilized by electrostatic interaction between fluorine atoms and their neighboring protons. LA - English DB - MTMT ER - TY - JOUR AU - Radis-Baptista, Gandhi TI - Cell-Penetrating Peptides Derived from Animal Venoms and Toxins JF - TOXINS J2 - TOXINS VL - 13 PY - 2021 IS - 2 PG - 25 SN - 2072-6651 DO - 10.3390/toxins13020147 UR - https://m2.mtmt.hu/api/publication/32370559 ID - 32370559 N1 - Cited By :12 Export Date: 27 January 2023 Correspondence Address: Rádis-Baptista, G.; Laboratory of Biochemistry and Biotechnology, Brazil; email: gandhi.radis@ufc.br AB - Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the ability to selectively interact with the cytoplasmic membrane of certain cell types, translocate across plasma membranes and accumulate in the cell cytoplasm, organelles (e.g., the nucleus and mitochondria) and other subcellular compartments. CPPs are either of natural origin or de novo designed and synthesized from segments and patches of larger proteins or designed by algorithms. With such intrinsic properties, along with membrane permeation, translocation and cellular uptake properties, CPPs can intracellularly convey diverse substances and nanomaterials, such as hydrophilic organic compounds and drugs, macromolecules (nucleic acids and proteins), nanoparticles (nanocrystals and polyplexes), metals and radionuclides, which can be covalently attached via CPP N- and C-terminals or through preparation of CPP complexes. A cumulative number of studies on animal toxins, primarily isolated from the venom of arthropods and snakes, have revealed the cell-penetrating activities of venom peptides and toxins, which can be harnessed for application in biomedicine and pharmaceutical biotechnology. In this review, I aimed to collate examples of peptides from animal venoms and toxic secretions that possess the ability to penetrate diverse types of cells. These venom CPPs have been chemically or structurally modified to enhance cell selectivity, bioavailability and a range of target applications. Herein, examples are listed and discussed, including cysteine-stabilized and linear, alpha-helical peptides, with cationic and amphipathic character, from the venom of insects (e.g., melittin, anoplin, mastoparans), arachnids (latarcin, lycosin, chlorotoxin, maurocalcine/imperatoxin homologs and wasabi receptor toxin), fish (pardaxins), amphibian (bombesin) and snakes (crotamine and cathelicidins). LA - English DB - MTMT ER - TY - JOUR AU - Rzeigui, Maha AU - Sahin, Zeynel AU - Roy, Olivier AU - Kucuk, Tugba AU - Goler, Omer AU - Atilla, Devrim AU - Khiari, Jameleddine AU - Dumoulin, Fabienne AU - Taillefumier, Claude TI - Peptoid-phthalocyanine architectures with different grafting positions: Synthetic strategy and photoproperties JF - DYES AND PIGMENTS J2 - DYES PIGMENTS VL - 189 PY - 2021 PG - 11 SN - 0143-7208 DO - 10.1016/j.dyepig.2020.109095 UR - https://m2.mtmt.hu/api/publication/32370557 ID - 32370557 N1 - Université Clermont Auvergne, CNRS, SIGMA Clermont, ICCF, Clermont-Ferrand, F-63000, France Université de Carthage, Faculté Des Sciences de Bizerte, Laboratoire de Chimie Organique et Analytique, ISEFC, Bardo, 2000, Tunisia Gebze Technical University, Chemistry Department, Gebze, Kocaeli 41400, Turkey Acıbadem Mehmet Ali Aydınlar University, Faculty of Engineering, Department of Medical Engineering, Istanbul, Turkey Export Date: 21 February 2022 CODEN: DYPID Correspondence Address: Khiari, J.; Gebze Technical University, Turkey; email: jamelkhiari@yahoo.fr Correspondence Address: Dumoulin, F.; Gebze Technical University, Turkey; email: Fabienne.Dumoulin@acibadem.edu.tr Correspondence Address: Taillefumier, C.; Université Clermont Auvergne, France; email: claude.taillefumier@uca.fr Funding details: Ministry of Higher Education and Scientific Research, MHESR Funding text 1: We thank Aurélie Job for HPLC measurements and Martin Leremboure (UCA Partner) for LCMS. M.R. was supported by a grant from the Ministry for Higher Education and Scientific Research of Tunisia . We acknowledge use of the UMS2008-IBSLor Biophysics and Structural Biology core facility at Université de Lorraine for CD measurements. AB - A monoazido Zn phthalocyanine has been grafted onto three different alkynyl-functionalized peptoid helices using copper-catalyzed azide-alkyne cycloaddition, demonstrating the feasibility of such conjugates. Their photoproperties have been examined relatively to the spatial geometry induced by the peptoid helix. LA - English DB - MTMT ER - TY - JOUR AU - Yokoo, H. AU - Hirano, M. AU - Misawa, T. AU - Demizu, Y. TI - Helical Antimicrobial Peptide Foldamers Containing Non-proteinogenic Amino Acids JF - CHEMMEDCHEM J2 - CHEMMEDCHEM VL - 16 PY - 2021 IS - 8 SP - 1226 EP - 1233 PG - 8 SN - 1860-7179 DO - 10.1002/cmdc.202000940 UR - https://m2.mtmt.hu/api/publication/31957074 ID - 31957074 N1 - Division of Organic Chemistry, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki, Kanagawa, 210-9501, Japan Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Yokohama, Kanagawa, 230-0045, Japan Export Date: 8 April 2021 CODEN: CHEMG Correspondence Address: Demizu, Y.; Division of Organic Chemistry, 3-25-26, Tonomachi, Kawasaki, Japan; email: demizu@nihs.go.jp Correspondence Address: Demizu, Y.; Graduate School of Medical Life Science, 1-7-29, Yokohama, Japan; email: demizu@nihs.go.jp AB - Antimicrobial peptides (AMPs) are potential novel therapeutic drugs against microbial infections. Most AMPs function by disrupting microbial membranes because of their amphipathic properties and ordered secondary structures. In this minireview, we describe recent efforts to develop helical AMP foldamers containing non-proteinogenic amino acids, such as α,α-disubstituted α-amino acids, β-amino acids, γ-amino acids, side-chain stapling and N-alkyl glycines. © 2021 Wiley-VCH GmbH LA - English DB - MTMT ER - TY - JOUR AU - Bogetti, A.T. AU - Piston, H.E. AU - Leung, J.M.G. AU - Cabalteja, C.C. AU - Yang, D.T. AU - Degrave, A.J. AU - Debiec, K.T. AU - Cerutti, D.S. AU - Case, D.A. AU - Horne, W.S. AU - Chong, L.T. TI - A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics JF - JOURNAL OF CHEMICAL PHYSICS J2 - J CHEM PHYS VL - 153 PY - 2020 IS - 6 SN - 0021-9606 DO - 10.1063/5.0019054 UR - https://m2.mtmt.hu/api/publication/32695481 ID - 32695481 N1 - Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, United States Molecular Biophysics and Structural Biology Graduate Program, University of Pittsburgh and Carnegie Mellon University, Pittsburgh, PA 15260, United States School of Computer Science and Engineering, University of Washington, Seattle, WA 98115, United States Department of Chemistry and Chemical Biology, Rutgers University, New Brunswick, NJ 008854, United States Cited By :3 Export Date: 21 February 2022 CODEN: JCPSA Correspondence Address: Horne, W.S.; Department of Chemistry, United States; email: horne@pitt.edu Correspondence Address: Chong, L.T.; Department of Chemistry, United States; email: ltchong@pitt.edu Funding details: National Science Foundation, NSF, CHE-1807301 Funding details: National Institutes of Health, NIH, 1R01GM115805-05, U54AI50470 Funding details: University of Pittsburgh Funding text 1: This work was supported by the University of Pittsburgh Arts and Sciences Graduate Fellowship to A.T.B., the NSF (Grant No. CHE-1807301) to L.T.C. and W.S.H., the NIH (Grant No. 1R01GM115805-05) to L.T.C., and the NIH (Grant No. U54AI50470) private clusters in the laboratory of D.A.C. Computational resources were provided by the University of Pittsburgh’s Center for Research Computing and private clusters in the CASE Laboratory. AB - We present a new force field, AMBER ff15ipq-m, for simulations of protein mimetics in applications from therapeutics to biomaterials. This force field is an expansion of the AMBER ff15ipq force field that was developed for canonical proteins and enables the modeling of four classes of artificial backbone units that are commonly used alongside natural α residues in blended or "heterogeneous"backbones: chirality-reversed D-α-residues, the Cα-methylated α-residue Aib, homologated β-residues (β3) bearing proteinogenic side chains, and two cyclic β residues (βcyc; APC and ACPC). The ff15ipq-m force field includes 472 unique atomic charges and 148 unique torsion terms. Consistent with the AMBER IPolQ lineage of force fields, the charges were derived using the Implicitly Polarized Charge (IPolQ) scheme in the presence of explicit solvent. To our knowledge, no general force field reported to date models the combination of artificial building blocks examined here. In addition, we have derived Karplus coefficients for the calculation of backbone amide J-coupling constants for β3Ala and ACPC β residues. The AMBER ff15ipq-m force field reproduces experimentally observed J-coupling constants in simple tetrapeptides and maintains the expected conformational propensities in reported structures of proteins/peptides containing the artificial building blocks of interest - all on the μs timescale. These encouraging results demonstrate the power and robustness of the IPolQ lineage of force fields in modeling the structure and dynamics of natural proteins as well as mimetics with protein-inspired artificial backbones in atomic detail. © 2020 Author(s). LA - English DB - MTMT ER - TY - JOUR AU - Darapaneni, Chandra Mohan AU - Ghosh, Pritam AU - Ghosh, Totan AU - Maayan, Galia TI - Unique β‐Turn Peptoid Structures and Their Application as Asymmetric Catalysts JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 26 PY - 2020 IS - 43 SP - 9573 EP - 9579 PG - 7 SN - 0947-6539 DO - 10.1002/chem.202000595 UR - https://m2.mtmt.hu/api/publication/31385327 ID - 31385327 N1 - Cited By :9 Export Date: 21 February 2022 CODEN: CEUJE Correspondence Address: Maayan, G.; Schulich Faculty of Chemistry, Israel; email: gm92@tx.technion.ac.il Chemicals/CAS: glycine, 56-40-6, 6000-43-7, 6000-44-8; Glycine; Peptidomimetics; Peptoids Funding details: Israel Science Foundation, ISF, 395/16 Funding text 1: This research was funded by the Israeli Science Foundation (ISF), grant number 395/16. The authors thank Mrs. Larisa Panz from the Schulich Faculty of Chemistry, Technion, for her support during MS analysis and simulations. P.G. is thankful to the Lady Davis Trust for supporting his postdoctoral fellowship. Funding text 2: This research was funded by the Israeli Science Foundation (ISF), grant number 395/16. The authors thank Mrs. Larisa Panz from the Schulich Faculty of Chemistry, Technion, for her support during MS analysis and simulations. P.G. is thankful to the Lady Davis Trust for supporting his postdoctoral fellowship. LA - English DB - MTMT ER - TY - JOUR AU - Nizami, Bilal AU - Bereczki-Szakál, Dorottya AU - Varró, Nikolett AU - El Battioui, Kamal AU - Udyavara Nagaraj, Vignesh AU - Szigyártó, Imola Csilla AU - Mándity, István AU - Beke-Somfai, Tamás TI - FoldamerDB: a database of peptidic foldamers JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 48 PY - 2020 IS - D1 SP - D1122 EP - D1128 SN - 0305-1048 DO - 10.1093/nar/gkz993 UR - https://m2.mtmt.hu/api/publication/30933404 ID - 30933404 N1 - Funding Agency and Grant Number: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP 16-1-2016-0007]; BIONANO [GINOP-2.3.2-15-2016-00017b] Funding text: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP 16-1-2016-0007]; BIONANO GINOP-2.3.2-15-2016-00017b. Funding for open access charge: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]. LA - English DB - MTMT ER - TY - JOUR AU - Quartararo, Anthony J. AU - Gates, Zachary P. AU - Somsen, Bente A. AU - Hartrampf, Nina AU - Ye, Xiyun AU - Shimada, Arisa AU - Kajihara, Yasuhiro AU - Ottmann, Christian AU - Pentelute, Bradley L. TI - Ultra-large chemical libraries for the discovery of high-affinity peptide binders JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 11 PY - 2020 IS - 1 SN - 2041-1723 DO - 10.1038/s41467-020-16920-3 UR - https://m2.mtmt.hu/api/publication/31385284 ID - 31385284 N1 - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, PO Box 513, Eindhoven, MB 5600, Netherlands Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan The Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, 500 Main Street, Cambridge, MA 02142, United States Center for Environmental Health Sciences, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, United States Broad Institute of MIT and Harvard, 415 Main Street, Cambridge, MA 02142, United States Cited By :26 Export Date: 21 February 2022 Correspondence Address: Pentelute, B.L.; Department of Chemistry, United States; email: blp@mit.edu Chemicals/CAS: 4 fluorophenylalanine, 51-65-0, 60-17-3; amino acid, 65072-01-7; diaminobutyric acid, 27252-32-0; hydroxyproline, 51-35-4, 6912-67-0; norvaline, 6600-40-4; ornithine, 70-26-8, 7006-33-9; phosphoserine, 407-41-0; carrier protein, 80700-39-6; Amino Acids; Antibodies, Monoclonal; Carrier Proteins; Peptide Library; Peptides; Proto-Oncogene Proteins c-mdm2; Small Molecule Libraries Funding details: T32 GM008334 Funding details: National Institute of General Medical Sciences, NIGMS, GM008334 Funding details: Defense Advanced Research Projects Agency, DARPA, 023504-001 Funding text 1: This work was supported by the NIH/NIGMS Interdepartmental Biotechnology Training Program (T32 GM008334 to A.J.Q.), the Defense Advanced Research Projects Agency (DARPA; Award 023504-001 to B.L.P.), and Calico (to B.L.P.). We gratefully acknowledge Anne Fischer and Tyler Stukenbroeker (DARPA) for their support and guidance; Earl Moore, Mark Paul, Louis Abruzzese, and David Sarracino for their technical assistance with nanoLC and Orbitrap mass spectrometry; and Eric Spooner, Marko Jovanovic, and Dan Maloney for their discussions regarding MS-based analysis and sequencing. We thank Joseph Brown for assistance with library synthesis, Suan Tuang for assistance with automated peptide synthesis, and Faycal Touti, Ethan Evans, and Alex Vinogradov for many fruitful scientific discussions. LA - English DB - MTMT ER - TY - JOUR AU - Stamatin, Yekaterina AU - Maayan, Galia TI - A Resin-Bound Peptoid as a Recyclable Heterogeneous Catalyst for Oxidation Reactions JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2020 PY - 2020 IS - 21 SP - 3147 EP - 3152 PG - 6 SN - 1434-193X DO - 10.1002/ejoc.201901739 UR - https://m2.mtmt.hu/api/publication/31385319 ID - 31385319 N1 - Cited By :5 Export Date: 21 February 2022 CODEN: EJOCF Correspondence Address: Maayan, G.; Schulich Faculty of Chemistry, Technion City, Israel; email: gm92@technion.ac.il Funding details: Israel Science Foundation, ISF, 395/16 Funding text 1: This research was funded by the Israeli Science Foundation (ISF), grant number 395/16. The authors thank Mr. Guilin Ruan from the Schulich Faculty of Chemistry, Technion, for performing some of the catalytic experiments. LA - English DB - MTMT ER - TY - JOUR AU - Szigyártó, Imola Csilla AU - Mihály, Judith AU - Wacha, András Ferenc AU - Bogdán, Dóra AU - Juhász, Tünde AU - Kohut, Gergely AU - Schlosser, Gitta (Vácziné) AU - Zsila, Ferenc AU - Urlacher, Vlada AU - Varga, Zoltán AU - Fulop, Ferenc AU - Bóta, Attila AU - Mándity, István AU - Beke-Somfai, Tamás TI - Membrane Active Janus-Oligomers of β 3 -Peptides JF - CHEMICAL SCIENCE J2 - CHEM SCI VL - 11 PY - 2020 IS - 26 SP - 6868 EP - 6881 PG - 14 SN - 2041-6520 DO - 10.1039/d0sc01344g UR - https://m2.mtmt.hu/api/publication/31355941 ID - 31355941 AB - Self-assembling peptides offer a versatile set of tools for bottom-up construction of supramolecular biomaterials. Among these compounds, non-natural peptidic foldamers experience increased focus due to their structural variability and lower sensitivity to enzymatic degradation. However, very little is known about their membrane properties and complex oligomeric assemblies - key areas for biomedical and technological applications. Here we designed short, acyclic beta(3)-peptide sequences with alternating amino acid stereoisomers to obtain non-helical molecules having hydrophilic charged residues on one side, and hydrophobic residues on the other side, with the N-terminus preventing formation of infinite fibrils. Our results indicate that these beta-peptides form small oligomers both in water and in lipid bilayers and are stabilized by intermolecular hydrogen bonds. In the presence of model membranes, they either prefer the headgroup regions or they insert between the lipid chains. Molecular dynamics (MD) simulations suggest the formation of two-layered bundles with their side chains facing opposite directions when compared in water and in model membranes. Analysis of the MD calculations showed hydrogen bonds inside each layer, however, not between the layers, indicating a dynamic assembly. Moreover, the aqueous form of these oligomers can host fluorescent probes as well as a hydrophobic molecule similarly toe.g.lipid transfer proteins. For the tested, peptides the mixed chirality pattern resulted in similar assemblies despite sequential differences. Based on this, it is hoped that the presented molecular framework will inspire similar oligomers with diverse functionality. LA - English DB - MTMT ER - TY - JOUR AU - Yokoo, Hidetomo AU - Misawa, Takashi AU - Demizu, Yosuke TI - De Novo Design of Cell‐penetrating Foldamers JF - CHEMICAL RECORD J2 - CHEM REC VL - 20 PY - 2020 IS - 9 SP - 912 EP - 921 PG - 10 SN - 1527-8999 DO - 10.1002/tcr.202000047 UR - https://m2.mtmt.hu/api/publication/31385325 ID - 31385325 N1 - Division of Organic Chemistry, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki, Kanagawa, 210-9501, Japan Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Yokohama, Kanagawa, 230-0045, Japan Cited By :5 Export Date: 21 February 2022 CODEN: CRHEA Correspondence Address: Misawa, T.; Division of Organic Chemistry, Japan; email: misawa@nihs.go.jp Correspondence Address: Demizu, Y.; Division of Organic Chemistry, Japan; email: demizu@nihs.go.jp Correspondence Address: Demizu, Y.; Graduate School of Medical Life Science, Japan; email: demizu@nihs.go.jp Chemicals/CAS: amino acid, 65072-01-7; proline, 147-85-3, 7005-20-1; urea, 57-13-6; Amino Acids; Cell-Penetrating Peptides; Drug Carriers; Peptides, Cyclic; Peptoids; Proline; Urea Funding details: Naito Foundation Funding details: Takeda Science Foundation Funding details: Sumitomo Foundation Funding details: Japan Agency for Medical Research and Development, AMED, 20mk0101120j0003 Funding details: Japan Society for the Promotion of Science, KAKEN, 17k08385, 18H05502, 18k14880 Funding details: Terumo Foundation for Life Sciences and Arts Funding details: NOVARTIS Foundation (Japan) for the Promotion of Science Funding text 1: This study was supported in part by grants from AMED under Grant Number 20mk0101120j0003, the Japan Society for the Promotion of Science (KAKENHI, Grants 18k14880 to T.M., 17k08385 and 18H05502 to Y.D.), TERUMO FOUNDATION for life sciences and ARTS (to Y.D.), Takeda Science foundation (to Y.D.), the Naito Foundation (to Y.D.), the Sumitomo Foundation (to Y.D.), and the NOVARTIS Foundation (Japan) for the Promotion of Science (to Y.D.). LA - English DB - MTMT ER - TY - JOUR AU - Amabili, Paolo AU - Calvaresi, Matteo AU - Martelli, Gianluca AU - Orena, Mario AU - Rinaldi, Samuele AU - Sgolastra, Federica TI - Imidazolidinone-Tethered alpha-Hydrazidopeptides - Synthesis and Conformational Investigation JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2019 PY - 2019 IS - 5 SP - 907 EP - 917 PG - 11 SN - 1434-193X DO - 10.1002/ejoc.201801427 UR - https://m2.mtmt.hu/api/publication/30452963 ID - 30452963 N1 - Funding Agency and Grant Number: Polytechnic University of Marche Funding text: Thanks are due to the Polytechnic University of Marche for the financial support ("Progetto Strategico di Ateneo"). AB - N-alpha-acylated beta(2,3)-3-azapeptides, or alpha-hydrazidopeptides, of different lengths were synthesized starting from a conformationally restricted imidazolidinone-tethered monomer. The preferential conformations of the oligomers were investigated by NMR and CD spectroscopy, supported by computational analysis. The experimental data clearly confirmed the tendency of these alpha-hydrazidopeptides to fold into a zig-zag (Z8) 8-helix conformation, whose stability is length-dependent, stabilized by the C=O(i)center dot center dot center dot H-N(i + 2) and N(i)center dot center dot center dot H-N(i + 1) intramolecular H-bonding pattern, as well as by non-standard C=O center dot center dot center dot H-C hydrogen bonds. LA - English DB - MTMT ER - TY - JOUR AU - de la Torre, Alexander F. AU - Ali, Akbar AU - Concepcion, Odette AU - Montero-Alejo, Ana L. AU - Muniz, Francisco M. AU - Jimenez, Claudio A. AU - Belmar, Julio AU - Luis Velazquez-Libera, Jose AU - Hernandez-Rodriguez, Erix W. AU - Caballero, Julio TI - A study of the cis-trans isomerization preference of N-alkylated peptides containing phosphorus in the side chain and backbone JF - NEW JOURNAL OF CHEMISTRY J2 - NEW J CHEM VL - 43 PY - 2019 IS - 32 SP - 12804 EP - 12813 PG - 10 SN - 1144-0546 DO - 10.1039/c9nj02234a UR - https://m2.mtmt.hu/api/publication/30989814 ID - 30989814 N1 - Departamento de Química Orgánica, Facultad de Ciencias Químicas, Universidad de Concepción, Concepción, Chile Department of Chemistry, University of Sargodha40100, Pakistan Departamento de Física, FCNMM, Universidad Tecnológica Metropolitana José Pedro, Alessandri 1242 Ñuñoa, Santiago, 780-0002, Chile Núcleo Milenio MULTIMAT, Chile Centro de Bioinformática y Simulación Molecular (CBSM), Universidad de Talca, 1 Poniente No. 1141 Casilla 721, Talca, Chile Escuela de Química y Farmacia, Facultad de Medicina, Universidad Católica Del Maule, Talca, 3460000, Chile Cited By :4 Export Date: 21 February 2022 CODEN: NJCHE Correspondence Address: De La Torre, A.F.; Departamento de Química Orgánica, Chile; email: afernandezd@udec.cl Chemicals/CAS: chloroform, 67-66-3; hydrogen, 12385-13-6, 1333-74-0; phosphorus, 7723-14-0; proton, 12408-02-5, 12586-59-3 Funding details: 3170003 Funding details: 11180984 Funding details: Fondo Nacional de Desarrollo Científico y Tecnológico, FONDECYT Funding text 1: This work was funded by CONICYT FONDECYT 3170003. A. F. de la Torre is grateful to FONDECYT project No. 3170003 for financial support. We also thank VRID technician K. Bustamante for NMR measurements at the University of Concepcion. Akbar Ali is thankful to TWAS–CNPq (3240266234) and HEC Pakistan (Project no. 21-2037/SRGP/R&D/HEC/2018). A. L. M. A. is thankful for a CONICYT/FONDECYT Iniciación 11180984 grant and to Núcleo Milenio MULTIMAT, Chile. Powered@NLHPC: This research was partially supported by the supercomputing infrastructure of the NLHPC (ECM-02). E. W. H. R. and J. C. are thankful to CONICYT FONDECYT/INACH/POSTDOCTORADO/No. 3170107. We are also thankful for the computing resources provided by the Department of Applied Physical Chemistry at the Universidad Autónoma de Madrid. AB - The current work provides a study on the cis-trans isomerization behaviour of N-alkylated peptides decorated with phosphonate ester groups. A Ugi four-component reaction was chosen for the synthesis of N-alkylated peptides, where almost only the cis isomer was detected when the phosphonate ester group was incorporated as an amine component in the side chain. However, the phosphonate ester group inserted in the backbone, as an isocyanide component, leads preferably to the trans isomer of this kind of peptides. The diverse behaviour of cis-trans isomerization has been explained via spectroscopic nuclear magnetic resonance analysis and computational calculations. LA - English DB - MTMT ER - TY - JOUR AU - Kulkarni, Ketav AU - Habila, Nathan AU - Del Borgo, Mark P. AU - Aguilar, Marie-Isabel TI - Novel Materials From the Supramolecular Self-Assembly of Short Helical beta(3)-Peptide Foldamers JF - FRONTIERS IN CHEMISTRY J2 - FRONT CHEM VL - 7 PY - 2019 PG - 12 SN - 2296-2646 DO - 10.3389/fchem.2019.00070 UR - https://m2.mtmt.hu/api/publication/30465244 ID - 30465244 AB - Self-assembly is the spontaneous organization of small components into higher-order structures facilitated by the collective balance of non-covalent interactions. Peptide-based self-assembly systems exploit the ability of peptides to adopt distinct secondary structures and have been used to produce a range of well-defined nanostructures, such as nanotubes, nanofibres, nanoribbons, nanospheres, nanotapes, and nanorods. While most of these systems involve self-assembly of alpha-peptides, more recently beta-peptides have also been reported to undergo supramolecular self-assembly, and have been used to produce materials-such as hydrogels-that are tailored for applications in tissue engineering, cell culture and drug delivery. This review provides an overview of self-assembled peptide nanostructures obtained via the supramolecular self-assembly of short beta-peptide foldamers with a specific focus on N-acetyl-beta(3)-peptides and their applications as bio- and nanomaterials. LA - English DB - MTMT ER - TY - JOUR AU - Mourtas, Spyridon AU - Gatos, Dimitrios AU - Barlos, Kleomenis TI - Solid-Phase Insertion of N-mercaptoalkylglycine Residues into Peptides JF - MOLECULES J2 - MOLECULES VL - 24 PY - 2019 IS - 23 SN - 1420-3049 DO - 10.3390/molecules24234261 UR - https://m2.mtmt.hu/api/publication/31385316 ID - 31385316 N1 - Export Date: 21 February 2022 CODEN: MOLEF Correspondence Address: Barlos, K.; Department of Chemistry, Greece; email: barlos@cblpatras.gr Chemicals/CAS: glycine, 56-40-6, 6000-43-7, 6000-44-8; thiol derivative, 13940-21-1; Glycine; Peptides; Peptoids; Sulfhydryl Compounds Funding details: University of Patras Funding text 1: Department of Chemistry, University of Patras, 26510 Rio Patras, Greece; s.mourtas@upatras.gr (S.M.); d.gatos@upatras.gr (D.G.) Institute of Chemical Engineering Sciences of the Foundation for Research and Technology Hellas (FORTH/IEC-HT), 26504 Rio Patras, Greece CBL-Patras, Patras Industrial Area, Block 1, 25018 Patras, Greece * Correspondence: barlos@cblpatras.gr; Tel.: +30-2610-647600; Fax: +30-2610-647316 Academic Editor: Theodore Tselios Received: 1 November 2019; Accepted: 20 November 2019; Published: 22 November 2019 LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Adrienn AU - Goldschmidt Gőz, Viktória AU - Pintér, István AU - Farkas, Viktor AU - Perczel, András TI - α/β-Chimera peptide synthesis with cyclic β-sugar amino acids: the efficient coupling protocol JF - AMINO ACIDS J2 - AMINO ACIDS VL - 51 PY - 2019 IS - 4 SP - 669 EP - 678 PG - 10 SN - 0939-4451 DO - 10.1007/s00726-019-02702-9 UR - https://m2.mtmt.hu/api/publication/30435771 ID - 30435771 N1 - Funding Agency and Grant Number: Eotvos Lorand University (ELTE); European Union; State of Hungary; European Regional Development Fund [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences Funding text: Open access funding provided by Eotvos Lorand University (ELTE). The authors wish to thank Dora K. Menyhard and Erno Keszei for consulting, Anita Kapros for the MS measurements, and Andras Lang and Daniel Horvath for helping 700 MHz NMR measurements. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. WoS:hiba:000463590400010 2019-04-21 12:29 cím nem egyezik Funding Agency and Grant Number: Eotvos Lorand University (ELTE); European UnionEuropean Commission; State of Hungary; European Regional Development FundEuropean Commission [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences Funding text: Open access funding provided by Eotvos Lorand University (ELTE). The authors wish to thank Dora K. Menyhard and Erno Keszei for consulting, Anita Kapros for the MS measurements, and Andras Lang and Daniel Horvath for helping 700 MHz NMR measurements. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. AB - The synthesis of α/β-chimeras comprises peptide bond formation from α- to β-, from β- to β-, and from β- to α-amino acid residues. The fine-tuned solid phase synthesis of –GXXG– chimera peptides containing the simplest achiral α-amino acid glycine and two cyclic SAAs of different ring size [X denoting cyclic β-Sugar Amino Acids (β-SAA)] is reported, variants containing Fmoc–RibAFU(ip)–OH a furanoid-, and Fmoc–GlcAPU(Me)–OH a pyranoid-type structural “Lego-element”. Systematic search for the best coupling strategy with both H–β-SAA–OHs is described, including the comparison of the different coupling reagents and conditions. Selecting the optimal reagent (from commonly used PyBOP, HATU and HOBt) was assisted by time-resolved 1H-NMR: formation and stability of the Fmoc protected active esters were compared. We found that PyBOP is the best choice for successfully coupling both H–β-SAA–OH prototypes. The present comparative results open a reasonable route for building efficiently various –β-SAA– containing homo- and heterooligomers. LA - English DB - MTMT ER - TY - JOUR AU - Oba, Makoto TI - Cell-Penetrating Peptide Foldamers: Drug-Delivery Tools JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 20 PY - 2019 IS - 16 SP - 2041 EP - 2045 PG - 5 SN - 1439-4227 DO - 10.1002/cbic.201900204 UR - https://m2.mtmt.hu/api/publication/30989813 ID - 30989813 N1 - Cited By :10 Export Date: 21 February 2022 CODEN: CBCHF Correspondence Address: Oba, M.; Graduate School of Biomedical Sciences, 1-14 Bunkyo-machi, Japan; email: moba@nagasaki-u.ac.jp Chemicals/CAS: 2 amino 2 methylpropionic acid, 62-57-7; C peptide, 59112-80-0; Cell-Penetrating Peptides AB - Highly efficient drug-delivery tools for membrane-impermeable compounds, proteins, and nucleic acids in living cells are useful in the fields of chemical biology and drug discovery, and such tools have been widely studied. One strategy in the development of novel drug-delivery tools is to utilize cell-penetrating peptide (CPP) foldamers. CPP foldamers are folded oligopeptides that possess cell membrane permeability. In recent decades, a wide variety of CPP foldamers have been reported by many groups. Herein, CPP foldamers are introduced and discussed from the viewpoints of component monomers (amino acids) and their application as drug-delivery tools. LA - English DB - MTMT ER - TY - JOUR AU - Oláh, Judit AU - Ovádi, Judit TI - Pharmacological targeting of α-synuclein and TPPP/p25 in Parkinson's disease. challenges and opportunities in a Nutshell. TS - challenges and opportunities in a Nutshell. JF - FEBS LETTERS J2 - FEBS LETT VL - 593 PY - 2019 IS - 13 SP - 1641 EP - 1653 PG - 13 SN - 0014-5793 DO - 10.1002/1873-3468.13464 UR - https://m2.mtmt.hu/api/publication/30706666 ID - 30706666 N1 - Journal Article; Review AB - With the aging of population, neurological disorders, and especially disorders involving defects in protein conformation (also known as proteopathies) pose a serious socio-economic problem. So far there is no effective treatment for most proteopathies, including Parkinson's disease (PD). The mechanism underlying PD pathogenesis is largely unknown, and the hallmark proteins, α-synuclein (SYN) and Tubulin Polymerization Promoting Protein (TPPP/p25) are challenging drug targets. These proteins are intrinsically disordered with high conformational plasticity, and have diverse physiological and pathological functions. In the healthy brain, SYN and TPPP/p25 occur in neurons and oligodendrocytes, respectively; however, in PD and multiple system atrophy, they are co-enriched and co-localized in both cell types, thereby marking pathogenesis. Although large inclusions appear at a late disease stage, small, soluble assemblies of SYN promoted by TPPP/p25 are pathogenic. In the light of these issues, we propose a new innovative strategy for the validation of a specific drug target based upon the identification of contact surfaces of the pathological SYN-TPPP/p25 complex that may lead to the development of peptidomimetic foldamers suitable for pharmaceutical intervention. This article is protected by copyright. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Rustagi, V. AU - Gomika, Udugamasooriya D. TI - A facile on-bead method for fully symmetric tetra-substituted DOTA derivatizations using peptoid moieties JF - BIOPOLYMERS J2 - BIOPOLYMERS VL - 110 PY - 2019 IS - 4 PG - 11 SN - 0006-3525 DO - 10.1002/bip.23249 UR - https://m2.mtmt.hu/api/publication/30367943 ID - 30367943 N1 - Funding Agency and Grant Number: University of Houston Funding text: University of Houston LA - English DB - MTMT ER - TY - JOUR AU - Baldessari, A. AU - Liñares, G.G. TI - Chemoenzymatic synthesis of nitrogen polymers with biomedical applications catalyzed by lipases JF - METHODS IN MOLECULAR BIOLOGY J2 - METHODS MOL BIOL VL - 1835 PY - 2018 SP - 359 EP - 376 PG - 18 SN - 1064-3745 DO - 10.1007/978-1-4939-8672-9_20 UR - https://m2.mtmt.hu/api/publication/32695486 ID - 32695486 N1 - Cited By :1 Export Date: 21 February 2022 Correspondence Address: Baldessari, A.; Facultad de Ciencias Exactas y Naturales, Argentina; email: alib@qo.fcen.uba.ar Chemicals/CAS: 1,3 propanediamine, 109-76-2; acrylic acid ethyl ester, 140-88-5; nitrogen, 7727-37-9; polycaprolactone, 24980-41-4, 25248-42-4; polypropylene, 25085-53-4, 9003-07-0; triacylglycerol lipase, 9001-62-1; Biocompatible Materials; Lipase; Nitrogen; Poly(amidoamine); Polyamines; Polymers AB - The application of Candida antarctica lipase B as catalyst in the synthesis of two examples of nitrogen polymers is described. Firstly, we report a novel linear polyamidoamine oligomer, obtained by polymerization of ethyl acrylate and N-methyl-1,3-diaminopropane, catalyzed by Candida antarctica lipase B immobilized on polypropylene. The second part of the chapter describes an efficient route for the synthesis of a novel β-peptoid oligomer with hydroxyalkyl pendant groups in the nitrogen atom, through the polymerization of ethyl N-(2-hydroxyethyl)-β-alaninate catalyzed by Candida antarctica lipase B physically adsorbed within a macroporous poly(methyl methacrylate-co-butyl methacrylate) resin. Moreover, two derivatives of the β-peptoid oligomer were prepared: by acetylation and by grafting polycaprolactone. This last process was performed through ring-opening polymerization of caprolactone from the β-peptoid pendant hydroxyl groups and afforded a brush copolymer. The products were blended with polycaprolactone to make films by solvent casting. The inclusion of the acyl derivatives of the β-peptoid to polycaprolactone affected the morphology of the film yielding micro- and nanostructured patterns. The obtained products showed biomedical applications. © Springer Science+Business Media, LLC, part of Springer Nature 2018. LA - English DB - MTMT ER - TY - JOUR AU - Dumonteil, Geoffrey AU - Bhattacharjee, Nicholus AU - Angelici, Gaetano AU - Roy, Olivier AU - Faure, Sophie AU - Jouffret, Laurent AU - Jolibois, Franck AU - Perrin, Lionel AU - Taillefumier, Claude TI - Exploring the Conformation of Mixed Cis-Trans alpha,beta-Oligopeptoids: A Joint Experimental and Computational Study JF - JOURNAL OF ORGANIC CHEMISTRY J2 - J ORG CHEM VL - 83 PY - 2018 IS - 12 SP - 6382 EP - 6396 PG - 15 SN - 0022-3263 DO - 10.1021/acs.joc.8b00606 UR - https://m2.mtmt.hu/api/publication/30452964 ID - 30452964 N1 - Université Clermont Auvergne, CNRS, SIGMA Clermont, ICCF, Clermont-Ferrand, F-63000, France Université de Toulouse-INSA-UPS, LPCNO, CNRS UMR 5215, 135 av Rangueil, Toulouse, F-31077, France Université de Lyon, Université Claude Bernard Lyon 1, CPE Lyon, INSA Lyon, ICBMS, CNRS UMR 5246, Equipe ITEMM, Bât Curien, 43 Boulevard du 11 Novembre 1918, Villeurbanne, 69622, France Cited By :10 Export Date: 21 February 2022 CODEN: JOCEA Correspondence Address: Jolibois, F.; Université de Toulouse-INSA-UPS, 135 av Rangueil, France; email: franck.jolibois@univ-tlse3.fr Chemicals/CAS: Biopolymers; Peptoids Funding details: European Commission, EC Funding details: Agence Nationale de la Recherche, ANR Funding details: European Regional Development Fund, FEDER Funding text 1: Aside from the interactions that involve the polar backbone carbonyl groups, additional weak interactions can develop between side chains. Recently, we have demonstrated that side-chain tBu···tBu interactions help promote helix folding of α-peptoids.18 In the present case, alternation of tBu and Ph side chains prevents tBu/tBu contact. However, a significant amount of interactions is observed between tBu and Ph side chains (Figure S9). As expected, these interactions are prominent between adjacent residues. However, peptoids that include αNPh residues show a larger amount of interactions than those containing βNPh residues. For tetramer 12, exclusively, an interaction is pinpointed between the tBu and Ph side chains at the N-and C-termini, respectively. This proximity is supported by the NOESY spectrum of tetramer 12 (Supporting Information). AB - The synthesis and conformational preferences of a set of new synthetic foldamers that combine both the alpha,beta-peptoid backbone and side chains that alternately promote cis- and trans-amide bond geometries have been achieved and addressed jointly by experiment and molecular modeling. Four sequence patterns were thus designed and referred to as cis-beta-trans-alpha, cis-alpha-trans-beta, trans-beta-cis-alpha, and trans-alpha-cis-beta. alpha- and beta NtBu monomers were used to enforce cis-amide bond geometries and alpha- and beta NPh monomers to promote trans-amides. NOESY and molecular modeling reveal that the trans-alpha-cis-beta and cis-beta-trans-alpha tetramers show a similar pattern of intramolecular weak interactions. The same holds for the cis-alpha-trans-beta and trans-beta-cis-alpha tetramers, but the interactions are different in nature than those identified in the trans-acis-beta-based oligomers. Interestingly, the trans-alpha-cis-beta peptoid architecture allows establishment of a larger amount of structure-stabilizing intramolecular interactions. LA - English DB - MTMT ER - TY - JOUR AU - Goel, Rahul AU - Garg, Charu AU - Gautam, Hemant Kumar AU - Sharma, Ashwani Kumar AU - Kumar, Pradeep AU - Gupta, Alka TI - Fabrication of cationic nanostructures from short self-assembling amphiphilic mixed alpha/beta-pentapeptide: Potential candidates for drug delivery, gene delivery, and antimicrobial applications JF - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES J2 - INT J BIOL MACROMOL VL - 111 PY - 2018 SP - 880 EP - 893 PG - 14 SN - 0141-8130 DO - 10.1016/j.ijbiomac.2018.01.079 UR - https://m2.mtmt.hu/api/publication/27609771 ID - 27609771 N1 - Department of Chemistry, Dyal Singh College, University of Delhi, Lodhi Road, New Delhi, 110003, India Nucleic Acids Research Laboratory, CSIR-Institute of Genomics and Integrative Biology, Delhi University Campus, Mall Road, Delhi, 110007, India Microbial Technology Laboratory, CSIR-Institute of Genomics and Integrative Biology, Sukhdev Vihar, Mathura Road, New Delhi, 110025, India Cited By :11 Export Date: 21 February 2022 CODEN: IJBMD Correspondence Address: Gupta, A.; Department of Chemistry, Lodhi Road, India; email: alkagupta@dsc.du.ac.in Chemicals/CAS: chloroquine, 132-73-0, 3545-67-3, 50-63-5, 54-05-7; curcumin, 458-37-7; levodopa, 59-92-7; Anti-Bacterial Agents; Antimicrobial Cationic Peptides Funding details: Council for Scientific and Industrial Research, CSIR Funding details: Council of Scientific and Industrial Research, India, CSIR, 0120, BSC 0112 Funding details: University Grants Commission, यूजीसी, 42-268/2013 Funding details: University Grants Committee, UGC, 42-268/2013 (SR) Funding text 1: The work is supported by the University Grants Commission (UGC major research project, 42-268/2013 (SR)), New Delhi. RG, CG, and AG would like to thank the Principal, Dyal Singh College for providing the required infrastructure for this work. PK and AKS thank financial support from the CSIR network projects (BSC 0112 and 0120). Authors gratefully acknowledge the support from USIC, University of Delhi for spectroscopic analysis of the compound. Funding text 2: The work is supported by the University Grants Commission (UGC major research project, 42-268/2013 (SR)), New Delhi. RG, CG, and AG would like to thank the Principal, Dyal Singh College for providing the required infrastructure for this work. PK and AKS thank financial support from the CSIR network projects ( BSC 0112 and 0120 ). Authors gratefully acknowledge the support from USIC, University of Delhi for spectroscopic analysis of the compound. AB - The present article describes designing and fabrication of nanostructures from a mixed a/β-pentapeptide, Lys-βAla-βAla-Lys-βAla, which majorly contains non-natural β-alanine residues in the backbone with two a-lysine residues at 1- and 4-positions. The amphiphilic pentapeptide showed the ability to self-assemble into cationic nanovesicles in an aqueous solution The average size of peptide nanostructures was found to be ~270 nm with a very high cationic charge of ~+40 mV. TEM micrographs revealed the average size of the same nanostructures ~80 nm bearing vesicular morphol. CD and FTIR spectroscopic studies on self-assembled pentapeptide hinted at random coil conformation which was also correlated with conformational search program using Hyper Chem 8.0. The pentapeptide nanostructures were then tested for encapsulation of hydrophobic model drug moieties, L-Dopa, and curcumin. Transfection efficiency of the generated cationic nanostructures was evaluated on HEK293 cells and compared the results with those obtained in the presence of chloroquine. The cytotoxicity assay performed using MTT depicted ~75-80% cell viability. The obtained nanostructures also gave pos. results against both Gram-neg. and Gram-pos. bacterial strains. Altogether the results advocate the promising potential of the pentapeptide foldamer, H-Lys-βAla-βAla-Lys-βAla-OEt, for drug and gene delivery applications along with the antimicrobial activity. LA - English DB - MTMT ER - TY - JOUR AU - Laurencin, Mathieu AU - Simon, Matthieu AU - Fleury, Yannick AU - Baudy-Floc'h, Michele AU - Bondon, Arnaud AU - Legrand, Baptiste TI - Selectivity Modulation and Structure of alpha/aza-beta(3) Cyclic Antimicrobial Peptides JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 24 PY - 2018 IS - 23 SP - 6191 EP - 6201 PG - 11 SN - 0947-6539 DO - 10.1002/chem.201800152 UR - https://m2.mtmt.hu/api/publication/27592892 ID - 27592892 LA - English DB - MTMT ER - TY - JOUR AU - Lockhart, Zachariah AU - Knipe, Peter C TI - Conformationally Programmable Chiral Foldamers with Compact and Extended Domains Controlled by Monomer Structure JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 57 PY - 2018 IS - 28 SP - 8478 EP - 8482 PG - 5 SN - 1433-7851 DO - 10.1002/anie.201802822 UR - https://m2.mtmt.hu/api/publication/27592715 ID - 27592715 N1 - Cited By :4 Export Date: 21 February 2022 CODEN: ACIEF Correspondence Address: Knipe, P.C.; School of Chemistry and Chemical Engineering, David Keir Building, United Kingdom; email: p.knipe@qub.ac.uk Funding details: Engineering and Physical Sciences Research Council, EPSRC, EP/R021481/1 Funding details: Royal Society, RG160614 Funding details: Queen's University Belfast Funding text 1: We acknowledge financial support from the Royal Society (RG160614, P.C.K.), the EPSRC (EP/R021481/1, P.C.K.) and Queen≫s University Belfast (start-up grant, P.C.K.), and thank Professor Eric V. Anslyn for helpful discussions in the preparation of this manuscript. Funding text 2: We acknowledge financial support from the Royal Society (RG160614, P.C.K.), the EPSRC (EP/R021481/1, P.C.K.) and Queen's University Belfast (start-up grant, P.C.K.), and thank Professor Eric V. Anslyn for helpful discussions in the preparation of this manuscript. LA - English DB - MTMT ER - TY - JOUR AU - Peraro, Leila AU - Deprey, Kirsten L. AU - Moser, Matthew K. AU - Zou, Zhongju AU - Ball, Haydn L. AU - Levine, Beth AU - Kritzer, Joshua A. TI - Cell Penetration Profiling Using the Chloroalkane Penetration Assay JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 140 PY - 2018 IS - 36 SP - 11360 EP - 11369 PG - 10 SN - 0002-7863 DO - 10.1021/jacs.8b06144 UR - https://m2.mtmt.hu/api/publication/30452965 ID - 30452965 N1 - Funding Agency and Grant Number: NIHUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [U19AI109725, R01GM127585]; NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [U19AI109725] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM127585] Funding Source: NIH RePORTER Funding text: The authors would like to thank D. Chenoweth and C. Aonbangkhen for cell lines and L. Walensky for reagents and helpful discussions. This work was supported by NIH U19AI109725 (B.L. and J.A.K.) and NIH R01GM127585 (J.A.K.). Department of Chemistry, Tufts University, Medford, MA 02155, United States Center for Autophagy Research, Department of Internal Medicine, University of Texas, Southwestern Medical Center, Dallas, TX 75230, United States Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, TX 75390, United States Department of Microbiology, University of Texas, Southwestern Medical Center, Dallas, TX 75390, United States Cited By :42 Export Date: 20 May 2021 CODEN: JACSA Correspondence Address: Kritzer, J.A.; Department of Chemistry, United States; email: joshua.kritzer@tufts.edu Chemicals/CAS: Cell-Penetrating Peptides; Hydrocarbons, Chlorinated Funding details: National Institutes of Health, NIH Funding details: National Institute of General Medical Sciences, NIGMS, R01GM127585 Funding details: National Institute of Allergy and Infectious Diseases, NIAID, U19AI109725 Funding text 1: This work was supported by NIH U19AI109725 (B.L. and J.A.K.) and NIH R01GM127585 (J.A.K.). Department of Chemistry, Tufts University, Medford, MA 02155, United States Center for Autophagy Research, Department of Internal Medicine, University of Texas, Southwestern Medical Center, Dallas, TX 75230, United States Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, TX 75390, United States Department of Microbiology, University of Texas, Southwestern Medical Center, Dallas, TX 75390, United States Cited By :42 Export Date: 21 May 2021 CODEN: JACSA Correspondence Address: Kritzer, J.A.; Department of Chemistry, United States; email: joshua.kritzer@tufts.edu Chemicals/CAS: Cell-Penetrating Peptides; Hydrocarbons, Chlorinated Funding details: National Institutes of Health, NIH Funding details: National Institute of General Medical Sciences, NIGMS, R01GM127585 Funding details: National Institute of Allergy and Infectious Diseases, NIAID, U19AI109725 Funding text 1: This work was supported by NIH U19AI109725 (B.L. and J.A.K.) and NIH R01GM127585 (J.A.K.). AB - Biotherapeutics are a promising class of molecules in drug discovery, but they are often limited to extracellular targets due to their poor cell penetration. High throughput cell penetration assays are required for the optimization of biotherapeutics for enhanced cell penetration. We developed a HaloTag-based assay called the chloroalkane penetration assay (CAPA), which is quantitative, high throughput, and compartment-specific. We demonstrate the ability of CAPA to profile extent of cytosolic penetration with respect to concentration, presence of serum, temperature, and time. We also used CAPA to investigate structure penetration relationships for bioactive stapled peptides and peptides fused to cell-penetrating sequences. CAPA is not only limited to measuring cytosolic penetration. Using a cell line where HaloTag is localized to the nucleus, we show quantitative measurement of nuclear penetration. Going forward, CAPA will be a valuable method for measuring and optimizing the cell penetration of biotherapeutics. LA - English DB - MTMT ER - TY - JOUR AU - Von Borowski, Rafael Gomes AU - Baggio Gnoatto, Simone Cristina AU - Macedo, Alexandre Jose AU - Gillet, Reynald TI - Promising Antibiofilm Activity of Peptidomimetics JF - FRONTIERS IN MICROBIOLOGY J2 - FRONT MICROBIOL VL - 9 PY - 2018 PG - 9 SN - 1664-302X DO - 10.3389/fmicb.2018.02157 UR - https://m2.mtmt.hu/api/publication/30452966 ID - 30452966 N1 - Univ Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR), UMR 6290, Rennes, France Programa de Pós-Graduação em Ciências Farmacêuticas, Faculdade de Farmácia, Biotechnology Center, Universidade Federal Do Rio Grande Do sul, Porto Alegre, Brazil Cited By :1 Export Date: 27 August 2019 Correspondence Address: Macedo, A.J.; Programa de Pós-Graduação em Ciências Farmacêuticas, Faculdade de Farmácia, Biotechnology Center, Universidade Federal Do Rio Grande Do sulBrazil; email: alexandre.macedo@ufrgs.br Funding details: Agence Nationale pour le Développement de la Recherche en Santé, -14-ASTR-0001 Funding details: Ministère de l’Enseignement Supérieur, de la Recherche Scientifique et des Technologies de l'Information et de la Communication Funding details: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior Funding details: Ministère des Affaires Étrangères Funding text 1: This study was funded by the CAPES-COFECUB program. The institutional partners of this partnership between Brazil and France are the Brazilian Ministry of Education’s CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior) agency, and the French Ministère de l’Europe et des Affaires étrangères (MEAE) and the Ministère de l’Enseignement supérieur, de la Recherche et de l’Innovation (MESRI). This work was also supported by the French Agence Nationale pour la Recherche and Direction Générale de l’Armement (#ANR-14-ASTR-0001). Univ Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR), UMR 6290, Rennes, France Programa de Pós-Graduação em Ciências Farmacêuticas, Faculdade de Farmácia, Biotechnology Center, Universidade Federal Do Rio Grande Do sul, Porto Alegre, Brazil Cited By :5 Export Date: 24 August 2020 Correspondence Address: Macedo, A.J.; Programa de Pós-Graduação em Ciências Farmacêuticas, Faculdade de Farmácia, Biotechnology Center, Universidade Federal Do Rio Grande Do sulBrazil; email: alexandre.macedo@ufrgs.br Export Date: 16 July 2021 AB - Pathogenic biofilms are a global health care concern, as they can cause extensive antibiotic resistance, morbidity, mortality, and thereby substantial economic loss. Scientific efforts have been made over the past few decades, but so far there is no effective treatment targeting the bacteria in biofilms. Antimicrobial peptidomimetics have been proposed as promising potential anti-biofilm agents. Indeed, these structurally enhanced molecules can mimic the action of peptides but are not susceptible to proteolysis or immunogenicity, the characteristic limitations of natural peptides. Here, we provide insights into antibiofilm peptidomimetic strategies and molecular targets, and discuss the design of two major peptidomimetics classes: AApeptides (N-acylated-N-aminoethyl-substituted peptides) and peptoids (N-substituted glycine units). In particular, we present details of their structural diversity and discuss the possible improvements that can be implemented in order to develop antibiofilm drug alternatives. LA - English DB - MTMT ER - TY - JOUR AU - Young, Sherri C TI - A Systematic Review of Antiamyloidogenic and Metal-Chelating Peptoids: Two Structural Motifs for the Treatment of Alzheimer's Disease JF - MOLECULES J2 - MOLECULES VL - 23 PY - 2018 IS - 2 PG - 14 SN - 1420-3049 DO - 10.3390/molecules23020296 UR - https://m2.mtmt.hu/api/publication/27336862 ID - 27336862 N1 - Cited By :9 Export Date: 21 February 2022 CODEN: MOLEF Correspondence Address: Young, S.C.; Department of Chemistry, 2400 Chew Street, United States; email: sherriyoung@muhlenberg.edu Chemicals/CAS: amyloid beta protein, 109770-29-8; Amyloid beta-Peptides; Chelating Agents; Peptoids LA - English DB - MTMT ER - TY - JOUR AU - Del Borgo, Mark P AU - Kulkarni, Ketav AU - Aguilar, Marie-Isabel TI - Unique Functional Materials Derived from beta-Amino Acid Oligomers JF - AUSTRALIAN JOURNAL OF CHEMISTRY J2 - AUST J CHEM VL - 70 PY - 2017 IS - 2 SP - 126 EP - 129 PG - 4 SN - 0004-9425 DO - 10.1071/CH16511 UR - https://m2.mtmt.hu/api/publication/26581834 ID - 26581834 LA - English DB - MTMT ER - TY - CHAP AU - Garcia-Fandiño, R. AU - Calvelo, M. AU - Granja, J.R. ED - Jerry, Atwood ED - George, W. Gokel ED - Len, Barbour TI - Pore- and Channel-Forming Peptides and Their Mimetics T2 - Comprehensive Supramolecular Chemistry II VL - 4 PB - Elsevier CY - Oxford SN - 9780128031988 T3 - Reference Module in Chemistry, Molecular Sciences and Chemical Engineering PY - 2017 SP - 539 EP - 573 PG - 35 DO - 10.1016/B978-0-12-409547-2.12546-6 UR - https://m2.mtmt.hu/api/publication/32695488 ID - 32695488 AB - Membrane channels are transmembrane-spanning structures that have an internal cavity that allow the migration of different ions and molecules. Inspired by the natural systems, chemists have created a variety of synthetic mimicries. Frequently, self-assembling methods were used to prepare the complex structure of these molecular channels. Although initially these synthetic assemblies were based on peptides, later, they were evolved to other structures facilitating the formation of channels. In this article, we review the most relevant strategies used for the preparation of relevant channel- forming architectures. © 2017 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - THES AU - Hegedüs, Zsófia TI - Molecular mimicry of conformationally diverse β-sheets by using α/β-peptide foldamers PB - Szegedi Tudományegyetem (SZTE) PY - 2017 SP - 54 DO - 10.14232/phd.3201 UR - https://m2.mtmt.hu/api/publication/3268249 ID - 3268249 LA - English DB - MTMT ER - TY - JOUR AU - Ilia, Ona AU - Antonio, Olivares Jose AU - Nolis, Pau AU - Ortuno, Rosa M TI - The relevance of the relative configuration in the folding of hybrid peptides containing beta-cyclobutane amino acids and gamma-amino-L-proline residues JF - TETRAHEDRON J2 - TETRAHEDRON VL - 73 PY - 2017 IS - 44 SP - 6286 EP - 6295 PG - 10 SN - 0040-4020 DO - 10.1016/j.tet.2017.09.011 UR - https://m2.mtmt.hu/api/publication/27100853 ID - 27100853 N1 - Funding Agency and Grant Number: Spanish Ministerio de Ciencia e InnovacionInstituto de Salud Carlos IIISpanish Government [CTQ2013- 43754-P, CTQ2016-77978-R]; UAB Funding text: Authors thank financial support from the Spanish Ministerio de Ciencia e Innovacion (CTQ2013- 43754-P and CTQ2016-77978-R). Time allocated in the Servei de Ressonancia Magnetica Nuclear (UAB) is gratefully acknowledged. Ms. Ester Calleja, Ms. Jennifer Marfa, Mr. Ramon Moreno and Mr. Jordi Solera are gratefully acknowledged for their helpful contributions. J.A.O. thanks the UAB for a predoctoral fellowship. LA - English DB - MTMT ER - TY - JOUR AU - Krieger, Viktoria AU - Ciglia, Emanuele AU - Thoma, Roland AU - Vasylyeva, Vera AU - Frieg, Benedikt AU - Amadeu, Nader de Sousa AU - Kurz, Thomas AU - Janiak, Christoph AU - Gohlke, Holger AU - Hansen, Finn K TI - -Aminoxy Peptoids: A Unique Peptoid Backbone with a Preference for cis-Amide Bonds JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 23 PY - 2017 IS - 15 SP - 3699 EP - 3707 PG - 9 SN - 0947-6539 DO - 10.1002/chem.201605100 UR - https://m2.mtmt.hu/api/publication/26581831 ID - 26581831 N1 - Institute of Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, Düsseldorf, 40225, Germany Institute of Inorganic and Structural Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, Düsseldorf, 40225, Germany Pharmaceutical/Medicinal Chemistry, Institute of Pharmacy, Leipzig University, Brüderstrasse 34, Leipzig, 04103, Germany Cited By :4 Export Date: 21 February 2022 CODEN: CEUJE Chemicals/CAS: amide, 17655-31-1; Amides; Peptoids Funding details: Verband der Chemischen Industrie, VCI Funding details: Deutsche Forschungsgemeinschaft, DFG, INST 208/704-1 FUGG Funding text 1: This work was supported by funds from the Fonds der Chemischen Industrie (to F.K.H.). The Deutsche Forschungsgemeinschaft (DFG) is acknowledged for funds used to purchase the UHR-TOF maXis 4G, Bruker Daltonics, Bremen HRMS instrument used in this research. Financial support by the Deutsche Forschungsgemeinschaft (DFG) for funds (INST 208/704-1 FUGG to H.G.) to purchase the hybrid computer cluster used in this study is gratefully acknowledged. Computational support and infrastructure was provided by the ?Center for Information and Media Technology? (ZIM) at the Heinrich Heine University D?sseldorf (HHU). We thank the Institute of Physical Biology at the HHU for providing us access to the CD spectrometer. LA - English DB - MTMT ER - TY - JOUR AU - Liu, Shan AU - Park, Shinae AU - Allington, Grant AU - Prelli, Frances AU - Sun, Yanjie AU - Marta-Ariza, Mitchell AU - Scholtzova, Henrieta AU - Biswas, Goutam AU - Brown, Bernard AU - Verghese, Philip B AU - Mehta, Pankaj D AU - Kwon, Yong-Uk AU - Wisniewski, Thomas TI - Targeting Apolipoprotein E/Amyloid beta Binding by Peptoid CPO_A beta 17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 7 PY - 2017 PG - 12 SN - 2045-2322 DO - 10.1038/s41598-017-08604-8 UR - https://m2.mtmt.hu/api/publication/26934093 ID - 26934093 N1 - Center for Cognitive Neurology, Department of Neurology, New York University, School of Medicine, New York, NY, United States Department of Chemistry and Nanoscience, Ewha Womans University, Seoul, South Korea Department of Chemistry, New York University, New York, NY, United States C2N Diagnostics, Center for Emerging Technologies, 4041 Forest Park Avenue, St. Louis, MO 63108, United States Department of Immunology, New York State Institute for Basic Research in Developmental Disabilities, New York, NY, United States Center for Cognitive Neurology, Departments of Neurology Psychiatry and Pathology, Neuroscience Institute, New York University, School of Medicine, New York, NY, United States Cited By :28 Export Date: 21 February 2022 Correspondence Address: Kwon, Y.-U.; Department of Chemistry and Nanoscience, South Korea; email: yukwon@ewha.ac.kr Chemicals/CAS: amyloid beta protein, 109770-29-8; Amyloid beta-Peptides; Apolipoproteins E; Neuroprotective Agents; Peptoids Funding details: National Institutes of Health, NIH Funding details: National Institute on Aging, NIA, P30AG008051 Funding details: National Institute of Neurological Disorders and Stroke, NINDS, R01NS073502 Funding details: National Research Foundation of Korea, NRF, 2012R1A1A2006417, 2015R1D1A1A01060628 Funding text 1: This work was supported by the NIH (grants: NS073502 and AG008051 to T.W.) and the National Research Foundation of Korea (grants: 2012R1A1A2006417 and 2015R1D1A1A01060628 to Y.U.K.). LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Nekkaa, Imane AU - Paragi, Gábor AU - Fülöp, Ferenc TI - Homochirality of beta-Peptides: A Significant Biomimetic Property of Unnatural Systems JF - CHEMISTRYOPEN J2 - CHEMISTRYOPEN VL - 6 PY - 2017 IS - 4 SP - 492 EP - 496 PG - 5 SN - 2191-1363 DO - 10.1002/open.201700078 UR - https://m2.mtmt.hu/api/publication/3266869 ID - 3266869 AB - Homochirality, an interesting phenomenon of life, is mainly an unresolved problem and was thought to be a property of living matter. Herein, we show that artificial beta-peptides have the tendency toward homochiral diastereoselective chain elongation. Chain-length-dependent stereochemical discrimination was investigated in the synthesis of foldamers with various side chains and secondary structures. It was found that there is a strong tendency toward the synthesis of homochiral oligomers. The size of the side chain drastically influenced the selectivity of the stereodiscriminative chain-elongation reaction. It is noteworthy that water as the co-solvent increases the selectivity. Such behavior is a novel fundamental biomimetic property of foldamers with a potential of future industrial application. LA - English DB - MTMT ER - TY - JOUR AU - Misawa, Takashi AU - Kanda, Yasunari AU - Demizu, Yosuke TI - Rational Design and Synthesis of Post-Functionalizable Peptide Foldamers as Helical Templates JF - BIOCONJUGATE CHEMISTRY J2 - BIOCONJUGATE CHEM VL - 28 PY - 2017 IS - 12 SP - 3029 EP - 3035 PG - 7 SN - 1043-1802 DO - 10.1021/acs.bioconjchem.7b00621 UR - https://m2.mtmt.hu/api/publication/27106717 ID - 27106717 LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Adrienn AU - Csordás, Barbara AU - Zsoldos-Mády, Virág AU - Pintér, István AU - Farkas, Viktor AU - Perczel, András TI - C-3 epimers of sugar amino acids as foldameric building blocks: improved synthesis, useful derivatives, coupling strategies JF - AMINO ACIDS J2 - AMINO ACIDS VL - 49 PY - 2017 IS - 2 SP - 223 EP - 240 PG - 18 SN - 0939-4451 DO - 10.1007/s00726-016-2346-5 UR - https://m2.mtmt.hu/api/publication/3134571 ID - 3134571 N1 - Megjegyzés-26507583 N1 Funding details: NK101072, OTKA, Országos Tudományos Kutatási Alapprogramok Funding Agency and Grant Number: Hungarian Scientific Research FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA NK101072] Funding text: The authors gratefully acknowledge Szebasztian Szaniszlo for his contribution to the preparative work and Prof. Imre G Csizmadia for helpful discussion. The authors wish to thank Laszlo Kocsis and Gabor Szirbik from ThalesNano Inc. (Budapest, Hungary) for their help and advice in hydrogenation reaction and for their support with the equipment, and Anita Kapros for her help in MS measurements. This work was supported by Grants from the Hungarian Scientific Research Fund (OTKA NK101072). AB - To obtain key sugar derivatives for making homooligomeric foldamers or α/β-chimera peptides, economic and multigram scale synthetic methods were to be developed. Though described in the literature, the cost-effective making of both 3-amino-3-deoxy-ribofuranuronic acid (H–t X–OH) and its C-3 epimeric stereoisomer, the 3-amino-3-deoxy-xylofuranuronic acid (H–c X–OH) from d-glucose is described here. The present synthetic route elaborated is (1) appropriate for large-scale synthesis; (2) reagent costs reduced (e.g. by a factor of 400); (3) yields optimized are ~80% or higher for all six consecutive steps concluding –t X– or –c X– and (4) reaction times shortened. Thus, a new synthetic route step-by-step optimized for yield, cost, time and purification is given both for d-xylo and d-ribo-amino-furanuronic acids using sustainable chemistry (e.g. less chromatography with organic solvents; using continuous-flow reactor). Our study encompasses necessary building blocks (e.g. –X–OMe, –X–OiPr, –X–NHMe, Fmoc–X–OH) and key coupling reactions making –Aaa–t X–Aaa– or –Aaa–t X–t X–Aaa– type “inserts”. Completed for both stereoisomers of X, including the newly synthesized Fmoc–c X–OH, producing longer oligomers for drug design and discovery is more of a reality than a wish. LA - English DB - MTMT ER - TY - JOUR AU - Opie, Christopher R AU - Kumagai, Naoya AU - Shibasaki, Masakatsu TI - Reversible Stereoselective Folding/Unfolding Fueled by the Interplay of Photoisomerism and Hydrogen Bonding JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 56 PY - 2017 IS - 12 SP - 3349 EP - 3353 PG - 5 SN - 1433-7851 DO - 10.1002/anie.201610279 UR - https://m2.mtmt.hu/api/publication/26581830 ID - 26581830 N1 - Cited By :6 Export Date: 21 February 2022 CODEN: ACIEF Correspondence Address: Kumagai, N.; Institute of Microbial Chemistry (BIKAKEN), 3-14-23 Kamiosaki, Shinagawa-ku, Japan; email: nkumagai@bikaken.or.jp Funding details: Japan Society for the Promotion of Science, KAKEN, 25713002, 26670009 Funding text 1: This work was financially supported by KAKENHI (No. 25713002, 26670009) from JSPS (to N.K.). Dr. Ryuichi Sawa, Yumiko Kubota, and Dr. Kiyoko Iijima are gratefully acknowledged for their assistance with the NMR analysis. We acknowledge Dr. Hidetoshi Noda for assistance with the MD simulations. We would like to thank anonymous reviewers for insightful suggestions which helped to improve the paper. LA - English DB - MTMT ER - TY - JOUR AU - Szefczyk, Monika AU - Weglarz-Tomczak, Ewelina AU - Fortuna, Paulina AU - Krzyszton, Agnieszka AU - Rudzinska-Szostak, Ewa AU - Berlicki, Lukasz TI - Controlling the Helix Handedness of alpha alpha beta-Peptide Foldamers through Sequence Shifting JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 56 PY - 2017 IS - 8 SP - 2087 EP - 2091 PG - 5 SN - 1433-7851 DO - 10.1002/anie.201610154 UR - https://m2.mtmt.hu/api/publication/26581832 ID - 26581832 LA - English DB - MTMT ER - TY - JOUR AU - Csordás, Barbara AU - Nagy, Adrienn AU - Harmat, Veronika AU - Zsoldos-Mády, Virág AU - Leveles, Ibolya AU - Pintér, István AU - Farkas, Viktor AU - Perczel, András TI - Origin of problems related to Staudinger reduction in carbopeptoid syntheses JF - AMINO ACIDS J2 - AMINO ACIDS VL - 48 PY - 2016 IS - 11 SP - 2619 EP - 2633 PG - 15 SN - 0939-4451 DO - 10.1007/s00726-016-2289-x UR - https://m2.mtmt.hu/api/publication/3098290 ID - 3098290 N1 - Megjegyzés-26182763 10.1007/s00726-016-2289-x AB - We report the solid phase synthesis of –GG-X-GG– type α/β-carbopeptoids incorporating RibAFU(ip) (1a, tX) or XylAFU(ip) (2a, cX) sugar amino acids. Though coupling efficacy is moderate, both the lengthier synthetic route using Fmoc derivative (e.g., Fmoc-RibAFU(ip)-OH) and the azido derivative (e.g., N3-RibAFU(ip)-OH) via Staudinger reaction with nBu3P can be successfully applied. Both X-ray diffraction, 1H- and 31P-NMR, and theoretical (QM) data support and explain why the application of Ph3P as Staudinger reagent is “ineffective” in the case of a cis stereoisomer, if cX is attached to the preceding residue with a peptide (–CONH–) bond. The failure of the polypeptide chain elongation with N3-cX originates from the “coincidence” of a steric crowdedness and an electronic effect disabling the mandatory nucleophilic attack during the hydrolysis of a quasi penta-coordinated triphenylphosphinimine. Nevertheless, the synthesis of the above α/β-chimera peptides as completed now by a new pathway via 1,2-O-isopropylidene-3-azido-3-deoxy-ribo- and -xylo-furanuronic acid (H-RibAFU(ip)-OH 1a and H-XylAFU(ip)-OH 2a) coupled with N-protected α-amino acids on solid phase could serve as useful examples and starting points of further synthetic efforts. © 2016 Springer-Verlag Wien LA - English DB - MTMT ER - TY - JOUR AU - Ellen, J Robertson AU - Caroline, Proulx AU - Jessica, K Su AU - Rita, L Garcia AU - Stan, Yoo AU - Eric, M Nehls AU - Michael, D Connolly AU - Laudann, Taravati AU - Ronald, N Zuckermann TI - Molecular Engineering of the Peptoid Nanosheet Hydrophobic Core JF - LANGMUIR J2 - LANGMUIR VL - 32 PY - 2016 IS - 45 SP - 11946 EP - 11957 PG - 12 SN - 0743-7463 DO - 10.1021/acs.langmuir.6b02735 UR - https://m2.mtmt.hu/api/publication/26277737 ID - 26277737 N1 - Cited By :20 Export Date: 21 February 2022 CODEN: LANGD Correspondence Address: Zuckermann, R.N.; Molecular Foundry, 1 Cyclotron Road, United States; email: rnzuckerman@lbl.gov Funding details: Defense Advanced Research Projects Agency, DARPA Funding details: Defense Threat Reduction Agency, DTRA, DTRA10027-15875 Funding text 1: This project was funded by the Defense Threat Reduction Agency under contract no. DTRA10027-15875 and the DARPA Fold F(x) program. LA - English DB - MTMT ER - TY - JOUR AU - Ellen, J Robertson AU - Eric, Michael Nehls AU - Ronald, N Zuckermann TI - Structure–Rheology Relationship in Nanosheet-Forming Peptoid Monolayers JF - LANGMUIR J2 - LANGMUIR VL - 32 PY - 2016 IS - 46 SP - 12146 EP - 12158 PG - 13 SN - 0743-7463 DO - 10.1021/acs.langmuir.6b02736 UR - https://m2.mtmt.hu/api/publication/26276180 ID - 26276180 N1 - Cited By :14 Export Date: 21 February 2022 CODEN: LANGD Correspondence Address: Zuckermann, R.N.; Molecular Foundry, 1 Cyclotron Road, United States; email: rnzuckermann@lbl.gov Funding details: U.S. Department of Energy, USDOE, DEAC02-05CH11231 Funding details: Defense Advanced Research Projects Agency, DARPA Funding details: Defense Threat Reduction Agency, DTRA, DTRA10027-15875 Funding details: Office of Science, SC Funding text 1: This project was funded by the Defense Threat Reduction Agency under contract no. DTRA10027-15875 and the DARPA Fold F(x) program. The work was conducted at the Molecular Foundry with support from the Advanced Light Source at Lawrence Berkeley National Laboratory, both of which are supported by the Office of Science, Office of Basic Energy Sciences, U.S. Department of Energy under contract no. DEAC02-05CH11231. LA - English DB - MTMT ER - TY - JOUR AU - Gopalakrishnan, Ranganath AU - Frolov, Andrey I AU - Knerr, Laurent AU - Drury, William J III AU - Valeur, Eric TI - Therapeutic Potential of Foldamers: From Chemical Biology Tools To Drug Candidates? JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 59 PY - 2016 IS - 21 SP - 9599 EP - 9621 PG - 23 SN - 0022-2623 DO - 10.1021/acs.jmedchem.6b00376 UR - https://m2.mtmt.hu/api/publication/26393033 ID - 26393033 LA - English DB - MTMT ER - TY - JOUR AU - Wojcik, Paulina AU - Berlicki, Lukasz TI - Peptide-based inhibitors of protein-protein interactions JF - BIOORGANIC & MEDICINAL CHEMISTRY LETTERS J2 - BIOORG MED CHEM LETT VL - 26 PY - 2016 IS - 3 SP - 707 EP - 713 PG - 7 SN - 0960-894X DO - 10.1016/j.bmcl.2015.12.084 UR - https://m2.mtmt.hu/api/publication/25447776 ID - 25447776 N1 - Cited By :101 Export Date: 21 February 2022 CODEN: BMCLE Correspondence Address: Berlicki, Ł.; Department of Bioorganic Chemistry, Wybrzeze Wyspiańskiego 27, Poland; email: lukasz.berlicki@pwr.edu.pl Chemicals/CAS: Peptides; Peptides, Cyclic; Proto-Oncogene Proteins c-mdm2; Tumor Suppressor Protein p53 Funding details: Narodowe Centrum Nauki, NCN Funding text 1: The work was financed by the National Science Centre , Poland (Grant No. DEC-2013/10/E/ST5/00625 ; Ł.B.), and Wroclaw Centre of Biotechnology , programme The Leading National Research Centre (KNOW) for years 2014–2018. Pictures were prepared using the Discovery Studio package (BIOVIA) used under a Polish country-wide license. The use of software resources (BIOVIA Discovery Studio program package) of the Wrocław Centre for Networking and Supercomputing is also kindly acknowledged. LA - English DB - MTMT ER -