Abstract
Four AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis. The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process, suggesting a molten-globule-like conformation after the first transition.
Keywords: Circular antimicrobial peptides, site-directed mutagenesis, lactic-acid bacteria, enterococci
Protein & Peptide Letters
Title: Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives
Volume: 17 Issue: 6
Author(s): Marina Sanchez-Hidalgo, Ana M Fernandez-Escamilla, Manuel Martinez-Bueno, Eva Valdivia, Luis Serrano and Mercedes Maqueda
Affiliation:
Keywords: Circular antimicrobial peptides, site-directed mutagenesis, lactic-acid bacteria, enterococci
Abstract: Four AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis. The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process, suggesting a molten-globule-like conformation after the first transition.
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Cite this article as:
Sanchez-Hidalgo Marina, M Fernandez-Escamilla Ana, Martinez-Bueno Manuel, Valdivia Eva, Serrano Luis and Maqueda Mercedes, Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives, Protein & Peptide Letters 2010; 17 (6) . https://dx.doi.org/10.2174/092986610791190390
DOI https://dx.doi.org/10.2174/092986610791190390 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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