Crabrolin, a natural antimicrobial peptide: structural properties
| Autor: | Aschi, M, Bozzi, A, Luzi, C, Bouchemal, N, Sette, M |
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| Přispěvatelé: | Dipartimento di Chimica, Ingegneria Chimica e Materiali, Università degli Studi dell'Aquila (UNIVAQ), Chimie, Structures et Propriétés de Biomatériaux et d'Agents Thérapeutiques (CSPBAT), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris 13 (UP13)-Institut Galilée-Université Sorbonne Paris Cité (USPC) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: | |
| Zdroj: | Journal of Peptide Science Journal of Peptide Science, 2017 |
| Popis: | International audience; A joint application of experimental and computational approaches has revealed the exceptionally high attitude of crabrolin, a 13-residue peptide with sequence FLPLILRKIVTAL-NH2, to adopt alpha-helix conformation not only in membrane-mimicking solvents but also in the presence of a not negligible amount of water. Our study shows that this propensity essentially resides in the intrinsic thermodynamic stability of alpha-helix conformation whose kinetic stability is drastically reduced in water solvent. Our analysis suggest that this is due to two effects enhanced by water; a more local effect consisting of the demolition of intra-peptide H-bonds, essential for the alpha-helix formation, and a bulk-electrostatic-effect favoring conformational states more polar than alpha-helix. |
| Databáze: | OpenAIRE |
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