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Abstract
The increasing resistance of microorganisms to antibiotics makes it a necessity that we search for new antimicrobial agents. Due to their genetically encoded nature, peptides are promising candidates for new antimicrobial drugs. Lantipeptide andalusicin exhibits significant antimicrobial activity against Gram-positive bacteria, making it a promising scaffold for the development of DNA-encoded libraries of lantibiotics. In this study, the modification reaction of andalusicin by class III lanthionine synthetase AncKC was reconstructed in a heterologous Escherichia coli system. The results obtained open possibilities for creating novel peptide- based antimicrobial agents.
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