Inhibition Effects of Some Bioactive Peroxovanadium Complexes on the Tyrosine Phosphatase

In order to study the structure-activity relationship and molecular mechanism of insulin-mimetic peroxovanadium complexes, the low-molecular-weight BHPTPase from bovine heart has been purified mainly by chromatography of DEAE-cellulose and Sephadex G-75, which was showed homogenicity on SDS-PAGE. Four bioactive peroxovanadium(pV) complexes bpV(ox), bpV(bipy), bpV(phen) and bpV(pic), [VO(O(2))(2)L](n-), where L = oxalic acid dianion(ox), bipyridine(bipy), 1,10-phenanthroline(phen), pyridine-2-carboxylic acid(pic) have been synthesized the bonding properties of center metal and its ligand were characterized by (51)V NMR, (13)C NMR, IR and elemental analysis. The complexes displayed remarkable inhibitory effects on the bovine heart tyrosine phosphatase. Their IC(50) were 0.22, 0.36 and 0.90 and 0.28 &mgr;mol/L, respectively. The structure-activity relationship of the complexes were discussed by their oxidizing ability and through the steric space hindrance of the organic ligands.