Conformational stability and activity of circular Enterocin AS-48 derivatives.

Marina Sánchez-Hidalgo, Ana M Fernández-Escamilla, Manuel Martínez-Bueno, Eva Valdivia, Luis Serrano, Mercedes Maqueda

Department de Microbiología, Facultad de Ciencias, Universidad de Granada, Spain.

Protein and peptide letters 2010 Jun

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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.

Citation

Marina Sánchez-Hidalgo, Ana M Fernández-Escamilla, Manuel Martínez-Bueno, Eva Valdivia, Luis Serrano, Mercedes Maqueda. Conformational stability and activity of circular Enterocin AS-48 derivatives. Protein and peptide letters. 2010 Jun;17(6):708-14