TY - JOUR AU - Bucci, Raffaella AU - Contini, Alessandro AU - Clerici, Francesca AU - Beccalli, Egle Maria AU - Formaggio, Fernando AU - Maffucci, Irene AU - Pellegrino, Sara AU - Gelmi, Maria Luisa TI - Fluoro-Aryl Substituted alpha,beta(2,3)-Peptides in the Development of Foldameric Antiparallel beta-Sheets: A Conformational Study JF - FRONTIERS IN CHEMISTRY J2 - FRONT CHEM VL - 7 PY - 2019 PG - 11 SN - 2296-2646 DO - 10.3389/fchem.2019.00192 UR - https://m2.mtmt.hu/api/publication/30909938 ID - 30909938 N1 - Department of Pharmaceutical Sciences (DISFARM), University of Milan, Milan, Italy Department of Chemistry, University of Padova, Padova, Italy CNRS UMR 7025, Génie Enzymatique et Cellulaire, Centre de Recherche de Royallieu, Compiègne, France Génie Enzymatique et Cellulaire, Centre de Recherche de Royallieu, Sorbonne Universités, Université de Technologie de Compiègne, Compiègne, France Cited By :12 Export Date: 21 February 2022 Correspondence Address: Gelmi, M.L.; Department of Pharmaceutical Sciences (DISFARM), Italy; email: marialuisa.gelmi@unimi.it Funding details: Horizon 2020 Framework Programme, H2020, 675527 AB - 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). LA - English DB - MTMT ER - TY - THES AU - Olajos, Gábor TI - Beta-amino acid substitutions in beta-sandwich model proteins PB - Szegedi Tudományegyetem (SZTE) PY - 2019 SP - 54 DO - 10.14232/phd.10055 UR - https://m2.mtmt.hu/api/publication/30808759 ID - 30808759 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 β-amino acids balance the stability and edge-protection of β-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 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 - 9780128031988 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 - BOOK ED - Jerry, Atwood ED - George, W. Gokel ED - Len, Barbour TI - Comprehensive Supramolecular Chemistry II T3 - Reference Module in Chemistry, Molecular Sciences and Chemical Engineering ET - 2 PB - Elsevier CY - Oxford PY - 2017 SP - 4568 SN - 9780128031988 UR - https://m2.mtmt.hu/api/publication/3129870 ID - 3129870 AB - 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. LA - English DB - MTMT ER -