Modification by Lanthionine Synthetase AncKC in a Heterologous <i>Escherichia coli</i> System
Nisso Z. MirzoevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationSofiya O. PipiyaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationYuliana A. MokrushinaDepartment of Chemistry, Lomonosov Moscow State University, Moscow, 119991 Russian FederationMarina V. SerebryakovaA.N. Belozersky Institute of Physicochemical Biology, Moscow, 119991 Russian FederationA. A. GrigorievaCenter of Life Sciences, Skolkovo Institute of Science and Technology; Institute of Gene Biology, Russian Academy of SciencesSvetlana DubileyCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, 121205 Russian FederationStanislav S. TerekhovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationI. V. SmirnovDepartment of Chemistry, Lomonosov Moscow State University, Moscow, 119991 Russian Federation
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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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