@article{MTMT:30909938,
	title = {Fluoro-Aryl Substituted alpha,beta(2,3)-Peptides in the Development of Foldameric Antiparallel beta-Sheets: A Conformational Study},
	url = {https://m2.mtmt.hu/api/publication/30909938},
	author = {Bucci, Raffaella and Contini, Alessandro and Clerici, Francesca and Beccalli, Egle Maria and Formaggio, Fernando and Maffucci, Irene and Pellegrino, Sara and Gelmi, Maria Luisa},
	doi = {10.3389/fchem.2019.00192},
	journal-iso = {FRONT CHEM},
	journal = {FRONTIERS IN CHEMISTRY},
	volume = {7},
	unique-id = {30909938},
	issn = {2296-2646},
	abstract = {alpha,beta(2,3)-Disteroisomeric foldamers of general formula Boc(S-Ala-beta-2R,3R-Fpg)(n) OMe or Boc(S-Ala-beta-2S,3S-Fpg)(n) OMe were prepared from both enantiomers of syn H-2-(2-F-Phe)-h-PheGly-OH (named beta-Fpg) and S-alanine. Our peptides show two appealing features for biomedical applications: the presence of fluorine, attractive for non-covalent interactions, and aryl groups, crucial for pi-stacking. A conformational study was performed, using IR, NMR and computational studies of diastereoisomeric tetra- and hexapeptides containing the beta(2,3)-amino acid in the R,R- and S,S-stereochemistry, respectively. We found that the stability of peptide conformation is dependent on the stereochemistry of the beta-amino acid. Combining S-Ala with beta-2R,3R-Fpg, a stable extended beta-strand conformation was obtained. Furthermore, beta-2R,3R-Fpg containing hexapeptide self-assembles to formantiparallel beta sheet structure stabilized by intermolecular H-bonds and pi, pi-interactions. These features make peptides containing the beta(2,3)-fluoro amino acid very appealing for the development of bioactive proteolytically stable foldameric beta-sheets as modulators of protein-protein interaction (PPI).},
	keywords = {FOLDAMERS; ANTIPARALLEL BETA-SHEET; beta(2,3)-diaryl-amino acid; alpha, beta(2,3)-peptide; extended peptide; conformational analyses},
	year = {2019},
	eissn = {2296-2646},
	orcid-numbers = {Pellegrino, Sara/0000-0002-2325-3583}
}

@mastersthesis{MTMT:30808759,
	title = {Beta-amino acid substitutions in beta-sandwich model proteins},
	url = {https://m2.mtmt.hu/api/publication/30808759},
	author = {Olajos, Gábor},
	doi = {10.14232/phd.10055},
	publisher = {SZTE},
	unique-id = {30808759},
	year = {2019},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891}
}

@article{MTMT:3399101,
	title = {Peripheral cyclic β-amino acids balance the stability and edge-protection of β-sandwiches},
	url = {https://m2.mtmt.hu/api/publication/3399101},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Szögi, Titanilla and Fülöp, Lívia and Martinek, Tamás},
	doi = {10.1039/c8ob01322e},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {16},
	unique-id = {3399101},
	issn = {1477-0520},
	abstract = {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.},
	keywords = {INHIBITORS; SECONDARY STRUCTURE; DE-NOVO DESIGN; HEAT-CAPACITY; ALPHA/BETA-PEPTIDES; protein–protein interactions; SHEET PROTEIN; FOLDING THERMODYNAMICS; GAMMA-PEPTIDES},
	year = {2018},
	eissn = {1477-0539},
	pages = {5492-5499},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066}
}

@{MTMT:3129878,
	title = {Molecular Recognition Using Foldamers},
	url = {https://m2.mtmt.hu/api/publication/3129878},
	author = {Hegedüs, Zsófia and Martinek, Tamás},
	booktitle = {Comprehensive Supramolecular Chemistry II},
	doi = {10.1016/B978-0-12-409547-2.12547-8},
	unique-id = {3129878},
	abstract = {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.},
	keywords = {PEPTIDES; SECONDARY STRUCTURE; HELIX; FOLDAMERS; Nucleic Acids; SHEET; protein–protein interactions; protein mimetics; β-Peptides; Aromatic oligoamides; PEPTOIDS; oligoureas; Azapeptides; Membrane-interacting foldamers; Molecular capsules},
	year = {2017},
	pages = {511-537},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}

@book{MTMT:3129870,
	title = {Comprehensive Supramolecular Chemistry II},
	url = {https://m2.mtmt.hu/api/publication/3129870},
	isbn = {9780128031995},
	editor = {Jerry, Atwood and George, W. Gokel and Len, Barbour},
	publisher = {Elsevier B.V.},
	unique-id = {3129870},
	abstract = {Comprehensive Supramolecular Chemistry II, Second Edition, Nine Volume Set is a ‘one-stop shop’ that covers supramolecular chemistry, a field that originated from the work of researchers in organic, inorganic and physical chemistry, with some biological influence.
		
		The original edition was structured to reflect, in part, the origin of the field. However, in the past two decades, the field has changed a great deal as reflected in this new work that covers the general principles of supramolecular chemistry and molecular recognition, experimental and computational methods in supramolecular chemistry, supramolecular receptors, dynamic supramolecular chemistry, supramolecular engineering, crystallographic (engineered) assemblies, sensors, imaging agents, devices and the latest in nanotechnology.
		
		Each section begins with an introduction by an expert in the field, who offers an initial perspective on the development of the field. Each article begins with outlining basic concepts before moving on to more advanced material.},
	year = {2017}
}