Crabrolin, a natural antimicrobial peptide: structural properties
Propriétés structurales de la craboline, un peptide antimicrobien naturel
Résumé
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.
Domaines
Biophysique
Origine : Fichiers produits par l'(les) auteur(s)
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