Phomopsin A

Short Summary : cyclic hexapeptide mycotoxin that binds ?-tubulin

Category : Cell Cycle/Checkpoint|Microtubule/Tubulin

Purity : 0.98

CAS Number : 64925-80-0

Formula : C36H45ClN6O12

Molecular Weight :

Molecular Weight : 789.2

SMILE : OC(/C(NC(/C(NC([C@H]1N(C([C@@H]2NC([C@H](C(C)=C)NC([C@@H](NC)[C@H](C3=CC(O[C@@]2(CC)C)=C(O)C(Cl)=C3)O)=O)=O)=O)CC=C1)=O)=C(CC)/C)=O)=CC(O)=O)=O

Solubility : Soluble in DMSO

Storage : Store at -20°C

Description : Phomopsin A is a cyclic hexapeptide mycotoxin that inhibits -tubulin. Phomopsins are a family of mycotoxins produced by the fungus Phomopsis leptostomiformis grows on lupins, which cause lupinosis, a severe liver disease of grazing animals [1][2]. Microtubules are one of the major components of the cytoskeleton that are essential in several cellular functions such as cell division and morphogenesis. – and -tubulins polymerize into microtubules. Phomopsin A is a cyclic hexapeptide mycotoxin that binds -tubulin in a vinca domain, partly overlapping with the site targeted by vinblastine and other tubulin inhibitors [2][3]. Phomopsin A noncompetitively inhibited the binding of radiolabeled vinblastine to tubulin with IC50 and Ki values of 0.8 M and 2.8 M, respectively. Phomopsin A potently inhibited tubulin-dependent GTP hydrolysis and nucleotide exchange on tubulin [2]. Phomopsin A, a vinca domain antimitotic peptide, also inhibited microtubule assembly [3][4]. Phomopsin A inhibited microtubule growth, modulated the dynamics of microtubules, and induced the self-association of tubulin dimers into single-walled rings and spirals [4].References:[1]. Hamel E. Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B. Pharmacol Ther. 1992;55(1):31-51.[2]. Cormier A, Marchand M, Ravelli RB, et al. Structural insight into the inhibition of tubulin by vinca domain peptide ligands. EMBO Rep. 2008 Nov;9(11):1101-6.[3]. Li Y, Kobayashi H, Hashimoto Y, et al. Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins. Biochem Biophys Res Commun. 1992 Sep 16;187(2):722-9.[4]. Mitra A, Sept D. Localization of the antimitotic peptide and depsipeptide binding site on beta-tubulin. Biochemistry. 2004 Nov 9;43(44):13955-62.

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