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P-113 Peptide: New experimental evidences on its biological activity and conformational insights from molecular dynamics simulations


  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at

  • Y.B.H. and J.F.S. contributed equally to this work.


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 Zn2+ 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.