Crabrolin, a natural antimicrobial peptide: structural properties

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 suggests 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. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

Experimental and computational approaches have revealed the high attitude of crabrolin, a 13‐residue peptide with sequence FLPLILRKIVTAL‐NH2, of folding in alpha‐helix in membrane‐mimicking solvents.

Source: Journal of Peptide Science - June 1, 2017 Category: Biochemistry Authors: Massimiliano Aschi, Argante Bozzi, Carla Luzi, Nadia Bouchemal, Marco Sette Tags: Research Article Source Type: research