Cyanopeptolins are cytotoxic serine protease inhibitors that was initially produced by species of cyanobacteria Microcystis. These peptides inhibit chymotrypsin, trypsin, plasmin, and elastase. Cyanopeptolins may also exhibit some antibacterial activity against gram positive and gram negative bacteria.
| Purity | ≥95% |
|---|---|
| Formula | C48H75ClN8O13 |
| Formula Wt. | 1007.61 |
| Store Temp | -20°C |
|---|---|
| Ship Temp | Blue Ice |
| Info Sheet | C9604 Info Sheet PDF |
|---|
Silva-Stenico ME, Rigonato J, Leal MG, et al. Non-ribosomal halogenated protease inhibitors from cyanobacterial isolates as attractive drug targets. Curr Med Chem. 2012;19(30):5205-13. PMID: 22934766.
Gademann K, Portmann C, Blom JF, et al. Multiple toxin production in the cyanobacterium microcystis: isolation of the toxic protease inhibitor cyanopeptolin 1020. J Nat Prod. 2010 May 28;73(5):980-4. PMID: 20405925.
Choi H, Oh SK, Yih W, et al. Cyanopeptoline CB071: a cyclic depsipeptide isolated from the freshwater cyanobacterium Aphanocapsa sp. Chem Pharm Bull (Tokyo). 2008 Aug;56(8):1191-3. PMID: 18670126.
von Elert E, Oberer L, Merkel P, et al. Cyanopeptolin 954, a chlorine-containing chymotrypsin inhibitor of Microcystis aeruginosa NIVA Cya 43. J Nat Prod. 2005 Sep;68(9):1324-7. PMID: 16180807.
Neumann U, Campos V, Cantarero S, et al. Co-occurrence of non-toxic (cyanopeptolin) and toxic (microcystin) peptides in a bloom of Microcystis sp. from a Chilean lake. Syst Appl Microbiol. 2000 Jun;23(2):191-7. PMID: 10930070.
