TY - JOUR AU - Drewniak, Magda AU - Weglarz-Tomczak, Ewelina AU - Ozga, Katarzyna AU - Rudzinska-Szostak, Ewa AU - Macegoniuk, Katarzyna AU - Tomczak, Jakub M. AU - Bejger, Magdalena AU - Rypniewski, Wojciech AU - Berlicki, Lukasz TI - Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics JF - BIOORGANIC CHEMISTRY J2 - BIOORG CHEM VL - 81 PY - 2018 SP - 356 EP - 361 PG - 6 SN - 0045-2068 DO - 10.1016/j.bioorg.2018.07.012 UR - https://m2.mtmt.hu/api/publication/30452990 ID - 30452990 AB - De novo designed helix-loop-helix peptide foldamers containing cis-2-aminocyclopentanecarboxylic acid residues were evaluated for their conformational stability and possible use in enzyme mimetic development. The correlation between hydrogen bond network size and conformational stability was demonstrated through CD and NMR spectroscopies. Molecules incorporating a Cys/His/Glu triad exhibited enzyme-like hydrolytic activity. LA - English DB - MTMT ER - TY - JOUR AU - Olajos, Gábor AU - Hetényi, Anasztázia AU - Wéber, Edit AU - Szögi, Titanilla AU - Fülöp, Lívia AU - Martinek, Tamás TI - Peripheral cyclic beta-amino acids balance the stability and edge-protection of beta-sandwiches JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 16 PY - 2018 IS - 30 SP - 5492 EP - 5499 PG - 8 SN - 1477-0520 DO - 10.1039/c8ob01322e UR - https://m2.mtmt.hu/api/publication/3399101 ID - 3399101 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [GINOP-2.3.3-15-2016-00010]\n Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and GINOP-2.3.3-15-2016-00010. E. W. thanks the Postdoctoral Fellowship Program 2014 of the Hungarian Academy of Sciences.\n Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [GINOP-2.3.3-15-2016-00010] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and GINOP-2.3.3-15-2016-00010. E. W. thanks the Postdoctoral Fellowship Program 2014 of the Hungarian Academy of Sciences. AB - Engineering water-soluble stand-alone beta-sandwich mimetics is a current challenge because of the difficulties associated with tailoring long-range interactions. In this work, single cis-(1R,2S)-2-aminocyclohexanecarboxylic acid mutations were introduced into the edge strands of the eight-stranded beta-sandwich mimetic structures from the betabellin family. Temperature-dependent NMR and CD measurements, together with thermodynamic analyses, demonstrated that the modified peripheral strands exhibited an irregular and partially disordered structure but were able to exert sufficient shielding on the hydrophobic core to retain the predominantly beta-sandwich structure. Although the frustrated interactions decreased the free energy of unfolding, the temperature of the maximum stabilities increased to or remained at physiologically relevant temperatures. We found that the irregular peripheral strands were able to prevent edge-to-edge association and fibril formation in the aggregation-prone model. These findings establish a beta-sandwich stabilization and aggregation inhibition approach, which does not interfere with the pillars of the peptide bond or change the net charge of the peptide. LA - English DB - MTMT ER - TY - CHAP AU - Hegedüs, Zsófia AU - Martinek, Tamás ED - Jerry, Atwood ED - George, W. Gokel ED - Len, Barbour TI - Molecular Recognition Using Foldamers T2 - Comprehensive Supramolecular Chemistry II PB - Elsevier CY - Oxford SN - 9780128031995 T3 - Reference Module in Chemistry, Molecular Sciences and Chemical Engineering PY - 2017 SP - 511 EP - 537 PG - 27 DO - 10.1016/B978-0-12-409547-2.12547-8 UR - https://m2.mtmt.hu/api/publication/3129878 ID - 3129878 AB - Self-organizing polymers (foldamers) that are capable of controlled molecular recognition are extensively investigated in supramolecular chemistry. The predictable shape and the modular synthesis of foldamers make them excellent tools with which to design and construct complementary interaction surfaces required for molecular recognition. The appropriate choice of monomeric unit patterns can lead to oligomers that recognize diverse interaction partners: cavities for small-molecule entrapment or the projection of functional groups from a well-defined scaffold to mimic complex structures such as protein surfaces. The construction of foldamers for protein recognition is a very attractive strategy for medicinal chemistry applications with promising results. In this article, foldamers that recognize small molecules, biomacromolecules, and membranes will be addressed with a brief general review of the structures and design strategies. © 2017 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Karancsiné Menyhárd, Dóra AU - Hudaky, I AU - Jákli, Imre AU - Juhasz, G AU - Perczel, András TI - Predictable Conformational Diversity in Foldamers of Sugar Amino Acids JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 57 PY - 2017 IS - 4 SP - 757 EP - 768 PG - 12 SN - 1549-9596 DO - 10.1021/acs.jcim.6b00488 UR - https://m2.mtmt.hu/api/publication/3239373 ID - 3239373 AB - A systematic conformational search was carried out for monomers and homohexamers of furanoid beta-amino, acids: cis-(S,R) and trans-(S,S) stereoisomers of aminocyclopentane carboxylic acid (ACPC), two different.aniinofuranuronic acids (AFU(alpha) and AFU(beta)), their isopropylidene derivatives (AFU(ip)), and the key intermediate beta-aminotetrahydrofurancarboxylic acid (ATFC). The stereochemistry of the building blocks was chosen to match that of the natural sugar amino acid (xylose and ribose) precursors (XylAFU and RibAFU). The results show that hexamera of cis-furanoid beta-amino acids show great variability: while hydrophobic.cyclopentane (cis-ACPC)(6) and hydrophilic (XylAFU(alpha/beta))(6) foldamers favor two different zigzagged conformation as hexaMers, the backbone fold turns into a helix in the case of (cis-ATFC)(6) (10 -helix) and (XylAFU(ip))(6) (14 -helix). Trans stereochemistry resulted in hexamers exclusively with the right-handed, helix conformation, (H-12(P))(6), regardless of their polarity. We found that the preferred.oligomeric structure of XylAFU(alpha/beta) is conformationally compatible 'with beta-pleated sheets, while that of the trans/(S,S) units matches with alpha-helices of proteins. 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 - Burslem, George M AU - Kyle, Hannah F AU - Breeze, Alexander L AU - Edwards, Thomas A AU - Nelson, Adam AU - Warriner, Stuart L AU - Wilson, Andrew J TI - Towards "bionic'' proteins: replacement of continuous sequences from HIF-1 alpha with proteomimetics to create functional p300 binding HIF-1 alpha mimics JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 52 PY - 2016 IS - 31 SP - 5421 EP - 5424 PG - 4 SN - 1359-7345 DO - 10.1039/c6cc01812b UR - https://m2.mtmt.hu/api/publication/25792592 ID - 25792592 LA - English DB - MTMT ER - TY - JOUR AU - Hegedüs, Zsófia AU - Makra, Ildikó AU - Imre, Norbert AU - Hetényi, Anasztázia AU - Mándity, István AU - Monostori, Éva AU - Martinek, Tamás TI - Foldameric probes for membrane interactions by induced β-sheet folding JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 52 PY - 2016 IS - 9 SP - 1891 EP - 1894 PG - 4 SN - 1359-7345 DO - 10.1039/C5CC09257D UR - https://m2.mtmt.hu/api/publication/2993079 ID - 2993079 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [TAMOP-4.2.6-14/1]\n Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and TAMOP-4.2.6-14/1. Csaba Vizler is gratefully acknowledged for providing the bEND.3 cell line.\n Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [TAMOP-4.2.6-14/1] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and TAMOP-4.2.6-14/1. Csaba Vizler is gratefully acknowledged for providing the bEND.3 cell line. AB - Design strategies were devised for alpha/beta-peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded beta-sheet in response to membrane interactions. Structure-activity relationships were investigated in the light of different beta-sheet folding levels. LA - English DB - MTMT ER - TY - JOUR AU - Makwana, Kamlesh Madhusudan AU - Mahalakshmi, Radhakrishnan TI - Stereopositional Outcome in the Packing of Dissimilar Aromatics in Designed -Hairpins JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 22 PY - 2016 IS - 12 SP - 4147 EP - 4156 PG - 10 SN - 0947-6539 DO - 10.1002/chem.201504428 UR - https://m2.mtmt.hu/api/publication/25792590 ID - 25792590 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Fülöp, Ferenc TI - An overview of peptide and peptoid foldamers in medicinal chemistry JF - EXPERT OPINION ON DRUG DISCOVERY J2 - EXPERT OPIN DRUG DIS VL - 10 PY - 2015 IS - 11 SP - 1163 EP - 1177 PG - 15 SN - 1746-0441 DO - 10.1517/17460441.2015.1076790 UR - https://m2.mtmt.hu/api/publication/2993085 ID - 2993085 N1 - Megjegyzés-25241274 N1 Funding Details: K 115731, OTKA, Országos Tudományos Kutatási Alapprogramok N1 Funding Details: PD 103994, OTKA, Országos Tudományos Kutatási Alapprogramok Hiányzó Jelleg: 'JOUR\n\nReview' Admin megjegyzés-25241274 tblcategory: (Category) ('JOUR\n\nReview') #Jelleg Megjegyzés-25241378 N1 Funding Details: K 115731, OTKA, Országos Tudományos Kutatási Alapprogramok N1 Funding Details: PD 103994, OTKA, Országos Tudományos Kutatási Alapprogramok Hiányzó Jelleg: 'JOUR\n\nReview' Admin megjegyzés-25241378 tblcategory: (Category) ('JOUR\n\nReview') #Jelleg LA - English DB - MTMT ER -