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 organiza

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.

The P-113 peptide: new experimental evidences on its biological activity and conformational insights from Molecular Dynamics simulations / Alessia Di, Giampaolo; Carla, Luzi; Casciaro, Bruno; Argante, Bozzi; Mangoni, Maria Luisa; Massimiliano, Aschi. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 102(2014), pp. 159-167. [10.1002/bip.22452]

The P-113 peptide: new experimental evidences on its biological activity and conformational insights from Molecular Dynamics simulations

CASCIARO, BRUNO;MANGONI, Maria Luisa;
2014

Abstract

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.
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 organiza
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/539397
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