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P‐113 Peptide: New experimental evidences on its biological activity and conformational insights from molecular dynamics simulations
Author(s) -
Giampaolo Alessia,
Luzi Carla,
Casciaro Bruno,
Bozzi Argante,
Luisa Mangoni Maria,
Aschi Massimiliano
Publication year - 2014
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22452
Subject(s) - chemistry , molecular dynamics , dynamics (music) , peptide , biophysics , computational biology , computational chemistry , biochemistry , physics , biology , acoustics
In this article, we report novel and additional results, both experimental and computational, obtained in our laboratories on the peptide P‐113. In particular, our experimental results indicate that this peptide is endowed with a high target‐cell selectivity towards yeast species, suggesting its potential development as a new drug against oral microbial infections. To provide additional structural insights, we performed several Molecular Dynamics simulations in different conditions. Results suggest that P‐113 is a rather compact species presumably because of its highly charged state as emerged from the dramatic increase of internal fluctuation occurring upon point‐mutation. The peptide turns out to adopt, in water, a beta‐hairpin‐like conformation and, in a more hydrophobic environment, is found to be in a (probably slow) equilibrium between α‐helix and hairpin conformations. Complexation with Zn 2+ induces a drastic mechanical stabilization, which prevents any conformational organization of the peptide into a biologically active state. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 159–167, 2014.