Title: Discovery, Structural Elucidation, and Functional Analysis of a Class I Lanthipeptide Candidate from Pseudoalteromonas sp. U16
Class I lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) with notable antimicrobial properties. With the rise of antimicrobial resistance remaining a critical global health issue, there is a high demand for novel therapeutics. Marine gram-negative bacteria, such as Pseudoalteromonas species, represent an underexplored reservoir of lanthipeptide biosynthetic potential. Many biosynthetic gene clusters (BGCs) in these bacteria remain cryptic under laboratory conditions. Therefore, this study aims to discover, elucidate the structure, and functionally characterize a novel Class I lanthipeptide from Pseudoalteromonas sp. U16. The approach integrates bioinformatic analysis of BGCs and heterologous co-expression of lanA, lanB, lanC, nisP, and glmU genes in E. coli, and downstream peptide isolation. Structural characterization will be performed using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Antimicrobial activity will be evaluated through bioactivity assays, and the resulting data will be correlated with LC-MS analyses to determine how post-translational modifications influence peptide activity and to assess its potential as a novel antimicrobial agent. The expected outcomes include identification of the mature peptide, detailed characterization of its post-translational modifications, and assessment of its bioactivity. By unlocking new antibiotic candidates and advancing knowledge of marine lanthipeptide biosynthesis, this study aims to make a meaningful contribution to the fight against antimicrobial resistance.
Keywords: Class I Lanthipeptide, RiPPs, antimicrobial resistance, antimicrobial activity, mature peptide, Pseudoalteromonas sp. U16, biosynthetic gene cluster (BGC)