Intensive Mutagenesis of the Nisin Hinge Leads to the Rational Design of Enhanced Derivatives

Abstract

Nisin A is the most extensively studied lantibiotic and has been used as a preservative by the food industry since 1953. This 34 amino acid peptide contains three dehydrated amino acids and five thioether rings. These rings, resulting from one lanthionine and four methyllanthionine bridges, confer the peptide with its unique structure. Nisin A has two… (More)
DOI: 10.1371/journal.pone.0079563

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