It was found to be a sulfur-containing amino acid; accordingly it was given the name lanthionine [wool (Latin: Lana), sulfur (Greek: theîon)].

Lanthionines have also been found in bacterial cell walls and are the components of a group of gene-encoded peptide antibiotics called lantibiotics, which includes nisin (a food preservative), subtilin, epidermin (effective against Staphylococcus and Streptococcus), and ancovenin (an enzyme inhibitor).

[3][4] A variety of syntheses of lanthionine have been published including sulfur extrusion from cystine,[5] ring opening of serine β-lactone,[4] and hetero-conjugate addition of cysteine to dehydroalanine.

[6] The sulfur extrusion method is, however, the only pathway for lanthionine that has been employed in the total synthesis of a lantibiotic.

Biosynthesis of the lanthionine bridge in peptidic natural products can be accomplished through a number of different pathways.