The increasing resistance of bacteria and fungi to the available antibiotic/antimycotic drugs urges for a search for new anti-infective compounds with new modes of action. In line of this, natural CAMPs represent promising and attractive candidates. Special attention has been devoted to frog-skin temporins, because of their short size (10-14 residues long) and their unique features. In particular, temporin-1Ta has the following properties: (i) it is mainly active on Gram-positive bacteria; (ii) it can synergize, when combined with temporin-1Tl, in inhibiting both gram-negative bacterial growth and the toxic effect of LPS; (iii) it preserves biological activity in the presence of serum; and (iv) it is practically not hemolytic. Rational design of CAMPs represents a straightforward approach to obtain a peptide with a better therapeutic index. Here, we used alanine scanning analogs to elucidate the contribution of the side chains of each amino acid residue to the peptide's antimicrobial and hemolytic activity. Beside providing insight into the biophysical attributes and the critical positions within the peptide sequence, which govern the antimicrobial/hemolytic activity of this temporin isoform, our studies assist in optimizing the design of temporin-based lead structures for the production of new anti-infective agents. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.

Alanine scanning analysis and structure-function relationships of the frog-skin antimicrobial peptide temporin-1Ta / Paolo, Grieco; Luca, Vincenzo; Luigia, Auriemma; Alfonso, Carotenuto; Maria Rosaria, Saviello; Pietro, Campiglia; Barra, Donatella; Ettore, Novellino; Mangoni, Maria Luisa. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - STAMPA. - 17:5(2011), pp. 358-365. ((Intervento presentato al convegno 12th Naples Workshop on Bioactive Peptides/2nd Italy-Korea Symposium on Antimicrobial Peptides tenutosi a Naples, ITALY nel JUN 04-07, 2010 [10.1002/psc.1350].

Alanine scanning analysis and structure-function relationships of the frog-skin antimicrobial peptide temporin-1Ta

LUCA, VINCENZO;BARRA, Donatella;MANGONI, Maria Luisa
2011

Abstract

The increasing resistance of bacteria and fungi to the available antibiotic/antimycotic drugs urges for a search for new anti-infective compounds with new modes of action. In line of this, natural CAMPs represent promising and attractive candidates. Special attention has been devoted to frog-skin temporins, because of their short size (10-14 residues long) and their unique features. In particular, temporin-1Ta has the following properties: (i) it is mainly active on Gram-positive bacteria; (ii) it can synergize, when combined with temporin-1Tl, in inhibiting both gram-negative bacterial growth and the toxic effect of LPS; (iii) it preserves biological activity in the presence of serum; and (iv) it is practically not hemolytic. Rational design of CAMPs represents a straightforward approach to obtain a peptide with a better therapeutic index. Here, we used alanine scanning analogs to elucidate the contribution of the side chains of each amino acid residue to the peptide's antimicrobial and hemolytic activity. Beside providing insight into the biophysical attributes and the critical positions within the peptide sequence, which govern the antimicrobial/hemolytic activity of this temporin isoform, our studies assist in optimizing the design of temporin-based lead structures for the production of new anti-infective agents. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
alanine scanning; antimicrobial peptides; antimicrobil peptide; frog skin; temporin
01 Pubblicazione su rivista::01a Articolo in rivista
Alanine scanning analysis and structure-function relationships of the frog-skin antimicrobial peptide temporin-1Ta / Paolo, Grieco; Luca, Vincenzo; Luigia, Auriemma; Alfonso, Carotenuto; Maria Rosaria, Saviello; Pietro, Campiglia; Barra, Donatella; Ettore, Novellino; Mangoni, Maria Luisa. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - STAMPA. - 17:5(2011), pp. 358-365. ((Intervento presentato al convegno 12th Naples Workshop on Bioactive Peptides/2nd Italy-Korea Symposium on Antimicrobial Peptides tenutosi a Naples, ITALY nel JUN 04-07, 2010 [10.1002/psc.1350].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/225770
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