@article{MTMT:34325417,
	title = {Display Selection of a Hybrid Foldamer-Peptide Macrocycle},
	url = {https://m2.mtmt.hu/api/publication/34325417},
	author = {Dengler, Sebastian and Howard, Ryan T. and Morozov, Vasily and Tsiamantas, Christos and Huang, Wei-En and Liu, Zhiwei and Dobrzanski, Christopher and Pophristic, Vojislava and Brameyer, Sophie and Douat, Celine and Suga, Hiroaki and Huc, Ivan},
	doi = {10.1002/anie.202308408},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	unique-id = {34325417},
	issn = {1433-7851},
	abstract = {Expanding the chemical diversity of peptide macrocycle libraries for display selection is desirable to improve their potential to bind biomolecular targets. We now have implemented a considerable expansion through a large aromatic helical foldamer inclusion. A foldamer was first identified that undergoes flexizyme-mediated tRNA acylation and that is capable of initiating ribosomal translation with yields sufficiently high to perform an mRNA display selection of macrocyclic foldamer-peptide hybrids. A hybrid macrocyclic nanomolar binder to the C-lobe of the E6AP HECT domain was selected that showed a highly converged peptide sequence. A crystal structure and molecular dynamics simulations revealed that both the peptide and foldamer are helical in an intriguing reciprocal stapling fashion. The strong residue convergence could be rationalized based on their involvement in specific interactions with the target protein. The foldamer stabilizes the peptide helix through stapling and through contacts with key residues. These results altogether represent a significant extension of the chemical space amenable to display selection and highlight possible benefits of inserting an aromatic foldamer into a peptide macrocycle for the purpose of protein recognition.},
	keywords = {PEPTIDES; FOLDAMERS; MACROCYCLES; protein recognition; Display Selection},
	year = {2023},
	eissn = {1521-3773},
	orcid-numbers = {Dengler, Sebastian/0000-0002-0770-0267; Tsiamantas, Christos/0000-0002-9326-7892; Douat, Celine/0000-0003-2678-1047}
}

@article{MTMT:34132519,
	title = {Sequence- and stereo-defined macromolecules: Properties and emerging functionalities},
	url = {https://m2.mtmt.hu/api/publication/34132519},
	author = {Szweda, Roza},
	doi = {10.1016/j.progpolymsci.2023.101737},
	journal-iso = {PROG POLYM SCI},
	journal = {PROGRESS IN POLYMER SCIENCE},
	volume = {145},
	unique-id = {34132519},
	issn = {0079-6700},
	year = {2023},
	eissn = {1873-1619},
	pages = {101737},
	orcid-numbers = {Szweda, Roza/0000-0003-2152-7656}
}

@article{MTMT:33413110,
	title = {Cavity-containing aromatic oligoamide foldamers and macrocycles: progress and future perspectives},
	url = {https://m2.mtmt.hu/api/publication/33413110},
	author = {Sobiech, Thomas A. and Zhong, Yulong and Gong, Bing},
	doi = {10.1039/d2ob01467j},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {20},
	unique-id = {33413110},
	issn = {1477-0520},
	abstract = {As a major class of foldamers, aromatic oligoamide foldamers have attracted intense interest. The rigidity of aromatic residues and amide linkages allows the development of foldamers with readily predictable, stable conformations. Aromatic oligoamide foldamers having backbones fully constrained by intramolecular hydrogen bonds have attracted wide attention. Depending on their lengths, such foldamers adopt crescent or helical conformations with highly negative inner cavities. Cyclizing the backbone of the aromatic oligoamides affords the corresponding macrocycles which are characterised by persistent shapes and non-deformable inner cavities. With their defined, inner cavities, such aromatic oligoamide foldamers and macrocycles have served as hosts for cationic and polar guests, and as transmembrane channels for transporting ions and molecules. Recent synthetic progress resulted in the construction of multi-turn hollow helices that offer three-dimensional inner pores with adjustable depth. Reducing the number of backbone-constraining hydrogen bonds leads to oligoamides which, with their partially constrained backbones, undergo either solvent- or guest-dependent folding. One class of such aromatic olgioamide foldamders, which offer multiple backbone amide NH groups as hydrogen-bond donors, are designed to bind anions with adjustable affinities.},
	year = {2022},
	eissn = {1477-0539},
	pages = {6962-6978},
	orcid-numbers = {Zhong, Yulong/0000-0002-4775-6855}
}

@article{MTMT:33413112,
	title = {alpha-Amino-iso-Butyric Acid Foldamers Terminated with Rhodium(I) N-Heterocyclic Carbene Catalysts},
	url = {https://m2.mtmt.hu/api/publication/33413112},
	author = {Tilly, David P. and Cullen, William and Zhong, Heng and Jamagne, Romain and Vitorica-Yrezabal, Inigo and Webb, Simon J.},
	doi = {10.1002/chem.202104293},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {28},
	unique-id = {33413112},
	issn = {0947-6539},
	abstract = {To investigate how remotely induced changes in ligand folding might affect catalysis by organometallic complexes, dynamic alpha-amino-iso-butyric acid (Aib) peptide foldamers bearing rhodium(I) N-heterocyclic carbene (NHC) complexes have been synthesized and studied. X-ray crystallography of a foldamer with an N-terminal azide and a C-terminal Rh(NHC)(Cl)(diene) complex showed a racemate with a chiral axis in the Rh(NHC) complex and a distorted 3(10) helical body. Replacing the azide with either one or two chiral L-alpha-methylvaline (L-alpha MeVal) residues gave diastereoisomeric foldamers that each possessed point, helical and axial chirality. NMR spectroscopy revealed an unequal ratio of diastereoisomers for some foldamers, indicating that the chiral conformational preference of the N-terminal residue(s) was relayed down the 1 nm helical body to the axially chiral Rh(NHC) complex. Although the remote chiral residue(s) did not affect the stereoselectivity of hydrosilylation reactions catalysed by these foldamers, these studies suggest a potential pathway towards remote conformational control of organometallic catalysts.},
	keywords = {FOLDAMERS; RHODIUM; conformation analysis; homogeneous catalysis; Carbene ligands},
	year = {2022},
	eissn = {1521-3765},
	orcid-numbers = {Vitorica-Yrezabal, Inigo/0000-0001-8806-150X}
}

@article{MTMT:32380638,
	title = {Evolution in non-peptide alpha-helix mimetics on the road to effective protein-protein interaction modulators},
	url = {https://m2.mtmt.hu/api/publication/32380638},
	author = {Algar, Sergio and Martin-Martinez, Mercedes and Gonzalez-Muniz, Rosario},
	doi = {10.1016/j.ejmech.2020.113015},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {211},
	unique-id = {32380638},
	issn = {0223-5234},
	abstract = {Modulation of interactome networks, essentially protein-protein interactions (PPIs), might represent valuable therapeutic approaches to different pathological conditions. Since a high percentage of PPIs are mediated by alpha-helical structures at the interacting surface, the development of compounds able to reproduce the amino acid side-chain organization of alpha-helices (e.g. stabilized alpha-helix peptides and beta-derivatives, proteomimetics, and alpha-helix small-molecule mimetics) focuses the attention of different research groups. This appraisal describes the recent progress in the non-peptide alpha-helix mimetics field, which has evolved from single-face to multi-face reproducing compounds and from oligomeric to monomeric scaffolds able to bear different substituents in similar spatial dispositions as the side-chains in canonical helices. Grouped by chemical structures, the review contemplates terphenyl-like molecules, oligobenzamides and heterocyclic analogues, benzamide-amino acid conjugates and non-oligomeric small-molecules mimetics, among others, and their effectiveness to stabilize/disrupt therapeutically relevant PPIs. The X-ray structures of a couple of oligomeric peptidomimetics and of some small-molecules complexed with the MDM2 protein, as well as the state of the art on their development in clinical trials, are also remarked. The discovery of a continuously increasing number of new diseaserelevant PPIs could offer future opportunities for these and other forthcoming alpha-helix mimetics. (C) 2020 Elsevier Masson SAS. All rights reserved.},
	keywords = {protein–protein interactions; Small-molecules; Non-peptide alpha-helix mimetics; Proteomimetics},
	year = {2021},
	eissn = {1768-3254},
	orcid-numbers = {Algar, Sergio/0000-0003-0933-5985}
}

@article{MTMT:32303604,
	title = {Influence of Terminal Functionality on the Crystal Packing Behaviour and Cytotoxicity of Aromatic Oligoamides},
	url = {https://m2.mtmt.hu/api/publication/32303604},
	author = {Delfosse, Pierre and Seaton, Colin C. and Male, Louise and Lord, Rianne M. and Pike, Sarah J.},
	doi = {10.3389/fchem.2021.709161},
	journal-iso = {FRONT CHEM},
	journal = {FRONTIERS IN CHEMISTRY},
	volume = {9},
	unique-id = {32303604},
	issn = {2296-2646},
	abstract = {The synthesis and characterization of three aromatic oligoamides, constructed from the same pyridyl carboxamide core but incorporating distinct end groups of acetyl (Ac) 1, tert-butyloxycarbonyl (Boc) 2 and amine 3 is reported. Single crystal X-ray diffraction analysis of 1-3 and a dimethylsulfoxide (DMSO) solvate of 2 (2-DMSO), has identified the presence of a range of intra- and intermolecular interactions including N-HMIDLINE HORIZONTAL ELLIPSISN, N-HMIDLINE HORIZONTAL ELLIPSISO=C and N-HMIDLINE HORIZONTAL ELLIPSISO=S(CH3)(2) hydrogen-bonding interactions, C-HMIDLINE HORIZONTAL ELLIPSIS pi interactions and off-set, face-to-face stacking pi-pi interactions that support the variety of slipped stack, herringbone and cofacial crystal packing arrangements observed in 1-3. Additionally, the cytotoxicity of this series of aromatic oligoamides was assessed against two human ovarian (A2780 and A2780cisR), two human breast (MCF-7 and MDA-MB-231) cancerous cell lines and one non-malignant human epithelial cell line (PNT-2), to investigate the influence of the terminal functionality of these aromatic oligoamides on their biological activity. The chemosensitivity results highlight that modification of the terminal group from Ac to Boc in 1 and 2 leads to a 3-fold increase in antiproliferative activity against the cisplatin-sensitive ovarian carcinoma cell line, A2780. The presence of the amine termini in 3 gave the only member of the series to display activity against the cisplatin-resistance ovarian carcinoma cell line, A2780cisR. Compound 2 is the lead candidate of this series, displaying high selectivity towards A2780 cancer cells when compared to non-malignant PNT-2 cells, with a selectivity index value >4.2. Importantly, this compound is more selective towards A2780 (cf. PNT-2) than the clinical platinum drugs oxaliplatin by > 2.6-fold and carboplatin by > 1.6-fold.},
	keywords = {CYTOTOXICITY; Crystallography; Aromatic oligoamides; Breast and ovarian cancer; Terminal group},
	year = {2021},
	eissn = {2296-2646}
}

@article{MTMT:32380640,
	title = {Natural and Synthetic Oligoarylamides: Privileged Structures for Medical Applications},
	url = {https://m2.mtmt.hu/api/publication/32380640},
	author = {Seedorf, Tim and Kirschning, Andreas and Solga, Danny},
	doi = {10.1002/chem.202005086},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {27},
	unique-id = {32380640},
	issn = {0947-6539},
	abstract = {The term "privileged structure" refers to a single molecular substructure or scaffold that can serve as a starting point for high-affinity ligands for more than one receptor type. In this report, a hitherto overlooked group of privileged substructures is addressed, namely aromatic oligoamides, for which there are natural models in the form of cystobactamids, albicidin, distamycin A, netropsin, and others. The aromatic and heteroaromatic core, together with a flexible selection of substituents, form conformationally well-defined scaffolds capable of specifically binding to conformationally well-defined regions of biomacromolecules such as helices in proteins or DNA often by acting as helices mimics themselves. As such, these aromatic oligoamides have already been employed to inhibit protein-protein and nucleic acid-protein interactions. This article is the first to bring together the scattered knowledge about aromatic oligoamides in connection with biomedical applications.},
	keywords = {DNA-BINDING; PROTEIN INTERACTIONS; FOLDAMERS; Aromatic oligoamides; protein–; cystobactamids; dystamycin},
	year = {2021},
	eissn = {1521-3765},
	pages = {7321-7339}
}

@{MTMT:33661624,
	title = {alpha-Helix Mimetics as Inhibitors of Protein-Protein Interactions},
	url = {https://m2.mtmt.hu/api/publication/33661624},
	author = {Wilson, A. J.},
	booktitle = {INHIBITORS OF PROTEIN-PROTEIN INTERACTIONS},
	unique-id = {33661624},
	keywords = {SOLID-PHASE SYNTHESIS; BETA-PEPTIDES; RATIONAL DESIGN; POTENT INHIBITORS; SMALL-MOLECULE INHIBITORS; Biochemistry & Molecular Biology; Chemistry, Medicinal; peptide foldamers; HORMONE-RECEPTOR; AROMATIC OLIGOAMIDE FOLDAMERS; PROTEOMIMETIC INHIBITORS},
	year = {2021},
	pages = {305-335}
}

@article{MTMT:31488181,
	title = {Small-Molecule Inhibitor Prevents Insulin Fibrillogenesis and Preserves Activity},
	url = {https://m2.mtmt.hu/api/publication/31488181},
	author = {Das, Anirban and Gangarde, Yogesh M. and Tomar, Viniti and Shinde, Omkar and Upadhyay, Tulsi and Alam, Sarfaraz and Ghosh, Sudipta and Chaudhary, Varun and Saraogi, Ishu},
	doi = {10.1021/acs.molpharmaceut.9b01080},
	journal-iso = {MOL PHARM},
	journal = {MOLECULAR PHARMACEUTICS},
	volume = {17},
	unique-id = {31488181},
	issn = {1543-8384},
	abstract = {Amyloidosis is a well-known but poorly understood phenomenon caused by the aggregation of proteins, often leading to pathological conditions. For example, the aggregation of insulin poses significant challenges during the preparation of pharmaceutical insulin formulations commonly used to treat diabetic patients. Therefore, it is essential to develop inhibitors of insulin aggregation for potential biomedical applications and for important mechanistic insights into amyloidogenic pathways. Here, we have identified a small molecule M1, which causes a dose-dependent reduction in insulin fibril formation. Biophysical analyses and docking results suggest that M1 likely binds to partially unfolded insulin intermediates. Further, M1-treated insulin had lower cytotoxicity and remained functionally active in regulating cell proliferation in cultured Drosophila wing epithelium. Thus, M1 is of great interest as a novel agent for inhibiting insulin aggregation during biopharmaceutical manufacturing.},
	keywords = {AGGREGATION; INHIBITORS; INSULIN; Docking; Hydrophobic interaction},
	year = {2020},
	eissn = {1543-8392},
	pages = {1827-1834},
	orcid-numbers = {Alam, Sarfaraz/0000-0002-7246-8687}
}

@article{MTMT:31424098,
	title = {Catalytic Foldamers: When the Structure Guides the Function},
	url = {https://m2.mtmt.hu/api/publication/31424098},
	author = {Legrand, Baptiste and Aguesseau-Kondrotas, Julie and Simon, Matthieu and Maillard, Ludovic},
	doi = {10.3390/catal10060700},
	journal-iso = {CATALYSTS},
	journal = {CATALYSTS},
	volume = {10},
	unique-id = {31424098},
	abstract = {Enzymes are predominantly proteins able to effectively and selectively catalyze highly complex biochemical reactions in mild reaction conditions. Nevertheless, they are limited to the arsenal of reactions that have emerged during natural evolution in compliance with their intrinsic nature, three-dimensional structures and dynamics. They optimally work in physiological conditions for a limited range of reactions, and thus exhibit a low tolerance for solvent and temperature conditions. Thede novodesign of synthetic highly stable enzymes able to catalyze a broad range of chemical reactions in variable conditions is a great challenge, which requires the development of programmable and finely tunable artificial tools. Interestingly, over the last two decades, chemists developed protein secondary structure mimics to achieve some desirable features of proteins, which are able to interfere with the biological processes. Such non-natural oligomers, so calledfoldamers, can adopt highly stable and predictable architectures and have extensively demonstrated their attractiveness for widespread applications in fields from biomedical to material science. Foldamer science was more recently considered to provide original solutions to thede novodesign of artificial enzymes. This review covers recent developments related to peptidomimetic foldamers with catalytic properties and the principles that have guided their design.},
	keywords = {COOPERATION; peptidomimetic; ORGANOCATALYST; foldamer},
	year = {2020},
	eissn = {2073-4344}
}

@article{MTMT:33661626,
	title = {Aromatic Helical Foldamers as Nucleophilic Catalysts for the Regioselective Acetylation of Octyl beta-d-Glucopyranoside},
	url = {https://m2.mtmt.hu/api/publication/33661626},
	author = {Song, Geunmoo and Jeong, Kyu-Sung},
	doi = {10.1002/cplu.202000685},
	journal-iso = {CHEMPLUSCHEM},
	journal = {CHEMPLUSCHEM},
	volume = {85},
	unique-id = {33661626},
	issn = {2192-6506},
	abstract = {Two indolocarbazole-naphthyridine foldamers 2 and 3 that fold into helical conformations were prepared. The 4-(N,N-dimethylamino)pyridine (DMAP) moiety was introduced at one end of the foldamer strands to develop foldamer-based catalysts for the site-selective acylation of polyols. These foldamers adopt helical conformations containing internal cavities capable of binding octyl beta-d-glucopyranoside. The association constants were determined to be 1.9 (+/- 0.1)x10(5) M-1 for 2 and 2.1 (+/- 0.1)x10(5) M-1 for 3 in CH2Cl2 at 25 degrees C. In the presence of DMAP, 2 or 3 as the catalysts, octyl beta-d-glucopyranoside was subjected to acetylation under identical reaction conditions. The DMAP-catalysed reaction afforded the random distribution of the monoacetylates (6-OAc : 4-OAc : 3-OAc : 2-OAc=33 : 24 : 41 : 2). In contrast, foldamers 2 and 3 led to the predominant formation of 6-OAc. The relative distributions were estimated to be 6-OAc : 4-OAc : 3-OAc=88 : 4 : 6 : similar to 0 with 2 and 6-OAc : 4-OAc : 3-OAc : 2-OAc=90 : 3 : 6 : 1 with 3.},
	keywords = {BINDING; ACYLATION; COMPLEX; RECEPTORS; RECOGNITION; FOLDAMERS; Carbohydrate; encapsulation; FUNCTIONALIZATION; HELICES; Carboxylate; nucleophilic catalysts; regioselective acylation},
	year = {2020},
	eissn = {2192-6506},
	pages = {2475-2481},
	orcid-numbers = {Jeong, Kyu-Sung/0000-0003-1023-1796}
}

@article{MTMT:31598466,
	title = {Proteomimetic surface fragments distinguish targets by function},
	url = {https://m2.mtmt.hu/api/publication/31598466},
	author = {Tököli, Attila and Mag, Beáta Zsófia and Bartus, Éva and Wéber, Edit and Szakonyi, Gerda and Simon, Márton and Czibula, Ágnes and Monostori, Éva and Nyitray, László and Martinek, Tamás},
	doi = {10.1039/d0sc03525d},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {11},
	unique-id = {31598466},
	issn = {2041-6520},
	year = {2020},
	eissn = {2041-6539},
	pages = {10390-10398},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Nyitray, László/0000-0003-4717-5994; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:31000418,
	title = {Crystal structure of a protein-aromatic foldamer composite: macromolecular chiral resolution},
	url = {https://m2.mtmt.hu/api/publication/31000418},
	author = {Alex, Jimi M. and Corvaglia, Valentina and Hu, Xiaobo and Engilberge, Sylvain and Huc, Ivan and Crowley, Peter B.},
	doi = {10.1039/c9cc05330a},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {55},
	unique-id = {31000418},
	issn = {1359-7345},
	abstract = {Co-crystallization of a 2 kDa tether-free sulfonated foldamer and the 13 kDa lysine-rich cytochrome c yielded a remarkable biohybrid assembly with chiral resolution of the foldamer helix handedness. In the crystal a similar to 5 nm foldamer stack was surrounded by eight molecules of protein. NMR and CD experiments suggest interesting differences in the solution state recognition processes.},
	keywords = {BINDING-SITE; COMPLEX; RECOGNITION; CYTOCHROME-C; OLIGOAMIDE-FOLDAMER},
	year = {2019},
	eissn = {1364-548X},
	pages = {11087-11090},
	orcid-numbers = {Corvaglia, Valentina/0000-0002-6180-5975}
}

@article{MTMT:31094010,
	title = {Bridged alpha-helix mimetic small molecules},
	url = {https://m2.mtmt.hu/api/publication/31094010},
	author = {Lee, Yeongju and Im, Haeri and Das, Sanket and Oh, Misook and Lee, Ji Hoon and Ham, Sihyun and Lim, Hyun-Suk},
	doi = {10.1039/c9cc03627j},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {55},
	unique-id = {31094010},
	issn = {1359-7345},
	abstract = {Herein, we report a strategy for generating conformationally restricted alpha-helix mimetic small molecules by introducing covalent bridges that limit rotation about the central axis of alpha-helix mimetics. We demonstrate that the bridged alpha-helix mimetics have enhanced binding affinity and specificity to the target protein due to the restricted conformation as well as extra interaction of the bridge with the protein surface.},
	year = {2019},
	eissn = {1364-548X},
	pages = {13311-13314}
}