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Abstract

In recent years, ribosomally synthesized and post-translationally modified peptides (RiPPs) have emerged as an important class of natural products in the fields of biology and medicine. RiPPs serve several biological functions including antimicrobial activity. Lasso peptides are one subfamily of RiPPs particularly known for their stability, making them ideal for applications as therapeutics. Structurally, lasso peptides feature a 7 to 9 amino acid N-terminal macrolactam ring, and the C-terminal segment of the peptide threads through the ring. This research aims to investigate a novel lasso peptide from Enterobacter, a 24 amino acid lasso peptide with a 9 membered ring suspected to have antimicrobial properties. The peptide was expressed in E. coli and analyzed using LCMS and HPLC. Potential unthreading of the peptide was noticed and further investigated, and it was found that the peptide exhibited unthreading behavior in the presence of acetonitrile. The threaded peptide was then purified for future antimicrobial tests.