Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives

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.

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