Self-assembly pathways in a triphenylalanine peptide capped with aromatic groups
| Autor: | Maria M. Pérez-Madrigal, Ana M. Gil, Jordi Casanovas, Ana I. Jiménez, Lorena P. Macor, Carlos Alemán |
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| Přispěvatelé: | Ministerio de Asuntos Económicos y Transformación Digital (España), Generalitat de Catalunya, Ministerio de Economía y Competitividad (España), Agencia Estatal de Investigación (España), Ministerio de Ciencia, Innovación y Universidades (España), European Commission, Gobierno de Aragón, Universitat Politècnica de Catalunya. Departament d'Enginyeria Química, Universitat Politècnica de Catalunya. IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies |
| Rok vydání: | 2022 |
| Předmět: |
Hierarchical structures
Triphenylalanine Phenylalanine Aromatic interactions Enginyeria biomèdica::Biomaterials [Àrees temàtiques de la UPC] Dipeptides Surfaces and Interfaces General Medicine Química supramolecular Enginyeria química [Àrees temàtiques de la UPC] Colloid and Surface Chemistry Supramolecular structures Materials biomèdics Beta-sheet Solvents Physical and Theoretical Chemistry Peptides Supramolecular chemistry Phenylalanine homopeptides Biomedical materials Biotechnology |
| Zdroj: | UPCommons. Portal del coneixement obert de la UPC Universitat Politècnica de Catalunya (UPC) |
| ISSN: | 0927-7765 |
| Popis: | Peptide derivatives and, most specifically, their self-assembled supramolecular structures are being considered in the design of novel biofunctional materials. Although the self-assembly of triphenylalanine homopeptides has been found to be more versatile than that of homopeptides containing an even number of residues (i.e. diphenylalanine and tetraphenylalanine), only uncapped triphenylalanine (FFF) and a highly aromatic analog blocked at both the N- and C-termini with fluorenyl-containing groups (Fmoc-FFF-OFm), have been deeply studied before. In this work, we have examined the self-assembly of a triphenylalanine derivative bearing 9-fluorenylmethyloxycarbonyl and benzyl ester end-capping groups at the N- and C-termini, respectively (Fmoc-FFF-OBzl). The antiparallel arrangement clearly dominates in β-sheets formed by Fmoc-FFF-OBzl, whereas the parallel and antiparallel dispositions are almost isoenergetic in Fmoc-FFF-OFm β-sheets and the parallel one is slightly favored for FFF. The effects of both the peptide concentration and the medium on the self-assembly process have been examined considering Fmoc-FFF-OBzl solutions in a wide variety of solvent:co-solvent mixtures. In addition, Fmoc-FFF-OBzl supramolecular structures have been compared to those obtained for FFF and Fmoc-FFF-OFm under identical experimental conditions. The strength of π-π stacking interactions involving the end-capping groups plays a crucial role in the nucleation and growth of supramolecular structures, which determines the resulting morphology. Finally, the influence of a non-invasive external stimulus, ultrasounds, on the nucleation and growth of supramolecular structures has been examined. Overall, FFF-based peptides provide a wide range of supramolecular structures that can be of interest in the biotechnological field. The authors gratefully acknowledge financial support provided by Ministerio de Asuntos Económicos y Transformación Digital, con Fondos de la Unión Europea - FEDER (MINECO/FEDER; RTI2018-098951-B-I00), Agència de Gestió d'Ajuts Universitaris i de Recerca (2017SGR359), and Gobierno de Aragón (research group Aminoácidos y Péptidos; E19_20R). M.M.P.-M. is thankful for the Junior Beatriz Galindo Fellowship (BG20/00216). |
| Databáze: | OpenAIRE |
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