Cinnamycin (syn: lanthiopeptin) is a high molecular weight tricyclic antibiotic produced by several species of Streptoverticillium cinnamoneus, first isolated in 1952.
Cinnamycin belongs to the class called lantibiotics (lanthionine-containing antibiotics) which are ribosomally synthesized peptides that are post-translationally modified. The Cinnamycin receptor is phosphatidylethanolamine (PE), a major compound found in many bacterial cell membranes.
Lantibiotics are grouped into two major categories: Type A lantibiotics (e.g. nisin, epidermin and Pep5) are flexible, elongated, amphipathic molecules which act mainly by forming pores in the bacterial cytoplasmic membrane. Type B lantibiotics (e.g. Cinnamycin, mersacidin, actagardine) have a rigid globular shape and inhibit enzymes by forming a complex with their membrane-bound substrates (ref).
Cinnamycin has antimicrobial properties, and cinnamy
cin-like peptides have inhibitory properties against angiotensin-converting enzyme, phospholipase A1, herpes simplex virus, and prostaglandin. Peptides such as duramycin and ancovenin also belong to the Cinnamycin family. Cinnamycin can be used in cystic fibrosis research.
Cinnamycin is soluble in ethanol, methanol, DMF and DMSO.
| Mechanism of Action | Cinnamycin is a potent indirect inhibitor of phospholipase A2, acting by specifically sequestering phosphatidylethanolamine (PE), a major component of the mammalian plasma cell membrane. Cinnamycin induces trans-bilayer phospholipid movement in cell membranes to expose internally bound PE. At high surface concentrations of PE, Cinnamycin induces membrane reorganization including membrane fusion and alteration of gross morphology. |
| Spectrum | Anaerobic bacteria, fungi, yeast. Lantibiotics are a group of antimicrobial peptides that are produced by and primarily act upon Gram-positive bacteria |
| Molecular Formula | C89H125N25O25S3 |
| References |
Brötz H, Sahl HG (2000). New insights into the mechanism of action of lantibiotics--diverse biological effects by binding to the same molecular target. J Antimicrob. Chemother. 46(1):1-6 PMID 10882681 Märki Fet al (1991) Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and Cinnamycin as indirect inhibitors of phospholipase A2. Biochem. Pharmacol. 42:2027 Fredenhagen A et al (1990) Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and Cinnamycin. J. Antibiot. 43:1403 Naruse NJ (1989) Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin. Antibiot. 42:837 |