isopetasin

Isopetasin is a synthetic peptide antibiotic that is structurally related to the natural antibiotic petasin. It was first synthesized in the 1980s and has since been studied for its potential antimicrobial properties. Isopetasin is a cyclic heptapeptide, consisting of seven amino acids arranged in a ring structure. Its primary sequence is Ac-Lys-Pro-Glu-Pro-Leu-Pro-NH2, which is similar to that of petasin but with an isoleucine residue replacing the leucine in the natural compound.

Isopetasin exhibits broad-spectrum antimicrobial activity, effective against both Gram-positive and Gram-negative bacteria, as well as fungi. Its mechanism of action involves inhibition of bacterial protein synthesis, specifically targeting the 50S ribosomal subunit. This mode of action is similar to that of other antibiotics, such as the macrolides and the aminoglycosides.

Isopetasin has been the subject of numerous studies, both in vitro and in vivo, to assess its potential as a therapeutic agent. However, its clinical use has been limited due to issues such as poor oral bioavailability and potential toxicity. Despite these challenges, isopetasin remains an interesting compound for further research, particularly in the context of antibiotic resistance and the development of new antimicrobial agents.