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Article Dans Une Revue Journal of Peptide Science Année : 2017

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
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Dates et versions

hal-02099883 , version 1 (15-04-2019)

Identifiants

  • HAL Id : hal-02099883 , version 1

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Massimiliano Aschi, Argante Bozzi, Carla Luzi, Nadia Bouchemal, Marco Sette. Crabrolin, a natural antimicrobial peptide: structural properties. Journal of Peptide Science, 2017. ⟨hal-02099883⟩
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