Citation: LI Peng-Yu, LU Li-Ping. PTPs Inhibition by Some Oxovanadium Complexes with Bioligands[J]. Chinese Journal of Inorganic Chemistry, ;2013, 29(9): 1830-1834. doi: 10.3969/j.issn.1001-4861.2013.00.229
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The inhibition of PTPs which dephosphorylate the insulin receptor, resulting in prolongation of insulin signaling, is involved in the mechanism of vanadiums insulin-sensitizing effects. Here, the speicies of vanadium complexes in the solution with bioligands to oxovanadium ions of 20:1 molar ratio are investigated by UV-Vis spectra, and their inhibition over protein tyrosine phosphatases are evaluated. The results show that in the solution, amino acids are coordinated to oxovanadium ions to form 2:1 vanadium complexes, but ascorbic acid, citric acid, iminodiacetic acid and malic acid form 1:1 vanadium complexes. The inhibitions against protein tyrosine phosphatases indicate among 19 systems of 20:1 molar ratio of bioligands to VO(Ⅱ), 14 systems exhibit strong inhibition over PTP1B (protein tyrosine phosphatase 1B) with IC50 of 0.12~0.63 μmol·L-1, and[VO(Phe)2] system displays strongest inhibition with IC50 of 0.07 μmol·L-1 while[VO(Arg)2],[VO(Oxalate)],[VO(Nitrilotriacetate] and[VO(Citrate)] systems show weaker inhibition with IC50 about 1.05, 1.41, 9.90 and 21.5 μmol·L-1, respectively. The selectivity of[VO(Arg)2],[VO(Tyr)2],[VO(Phe)2],[VO(Malate)],[VO(Lactate)] and[VO(Citrate)] systems over PTP1B, TCPTP (T-cell protein tyrosine phosphatase), HePTP (Hematopoietic protein tyrosine phosphatase) and SHP-1 (Src homology phosphatase 1) show the inhibitions against four PTPs are varied with the change of the bioligands, suggesting the structures of the bioligands influence the potency of the PTPs inhibition and the selectivity.
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