Lantibiotics are peptide-derived antimicrobial agents that are ribosomally synthesized and posttranslationally modified to their biologically active forms. The post-translational modifications involve the formation of dehydroalanine and dehydrobutyrine residues and the subsequent attack of cysteines within the peptide onto the dehydro amino acids. This generates the so-called lanthionine and methyllanthionine thioethers that have given lantibiotics their name. One family member, nisin, has attracted much attention recently due to its novel mechanism of action including specific binding to the bacterial cell wall precursor lipid II, followed by membrane permeabilization. Nisin has been commercially used as a food preservative, while other lantibiotics show promising activity against bacterial infections. This mini-review focuses on the recent developments in the characterization of these enzymes as well as the progress in chemical synthesis of lanthionine containing peptides.
Keywords: lanthionine, lantibiotics, nisin, lacticin, dehydroalanine, dehydrobutyrine
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