Synthesis, Characterization And Biological Properties For New Type Of Vanadyl Complexes

In recent years, the hypoglycemic activity of vanadium complex has been more and more attented. The mechanism is generally considered competitive binding protein tyrosine phosphatase 1B, inhibiting the activity of PTP1B. So as to obtained the effects of hypoglycemic.In this present, six kinds of vanadyl complexes have been synthesized, which were vanadyl oxalate (1), oxalic acid peroxovadate (2), vanadyl malate dihydrate (3), vanadyl acetylacetonate (4), acetylacetone-(8-hydroxyqunoline) vanadyl (5),2-(8-hydroxyqunoline) vanadyl (6). Particularly, the complexes 5 and 6 were firstly synthesized. The structures of them were characterized with the IR, NMR and differential thermal analysis etc.At the second part, the interaction between complex 2 and 6 and glutathione(GSH) was carried out by UV-Vis spectra, and the two complexes could be react with the GSH and get stable new species. The results showed that these complexes can interact with the sulfur-containing biomolecula, and the binding site may be the-SH of Cysteine, which was provided the experimental base for the in vivo biological activity of these complexes. But the reaction mechanism is unclear.Subseqently, the reaction of complexes 2,4,5,6 and were measured comparison to that of VOSO4. The complexes can inhibited the substrate binding of PTP1B in some extent. Determinning the type of inhibition. Based on the results of IC50, the inhibitive mechanism may be purposed.