Lantipeptide (Lantibiotic)
A class of antimicrobial peptides containing unusual amino acids formed through post-translational modification, including lanthionine bridges. Nisin is the best-known lantibiotic, used as a food preservative. Lantipeptides represent a structurally distinct class of naturally occurring antimicrobial peptides.
Technical Context
Lantipeptides are ribosomally synthesised and post-translationally modified peptides (RiPPs) containing lanthionine (Lan) and/or methyllanthionine (MeLan) bridges — thioether crosslinks formed by post-translational dehydration and cyclisation of serine/threonine with cysteine. These crosslinks create conformationally constrained ring structures. Nisin (34 amino acids, 5 ring structures) is the most extensively studied lantibiotic — used as a food preservative (E234) for over 50 years with no significant resistance development. Nisin's mechanism: binds lipid II (the same target as vancomycin) with high affinity and forms pores in the bacterial membrane — a dual mechanism. Pharmaceutical lantibiotic development targets: MRSA, VRE, and other drug-resistant gram-positive pathogens. The complexity of lanthionine bridge formation makes chemical synthesis challenging — production typically uses fermentation of the producing organism.