| Protein tyrosine phosphatase 1B (PTP1B) is one of the protein tyrosinephosphatase (PTPs) family and the first separated PTP. Protein tyrosinephosphatase 1B, as a typical non-receptor type member of the family of PTPs,is a key element in the negative regulation of insulin signaling pathway, andalso has been a novel drug target for diabetes and obesity.Ⅱ-type diabetes is a sort of metabolize turbulence disease. It exhibitsimpaired insulin action, or insulin resistance and the absence of insulin andits acceptor at molecular level. The insulin-impedance is a main reason forcausing the typeⅡdiabetes, and can cause the organism to be fat, discoverthe protein tyrosine phosphatase 1B (PTP1B) is closely related to this course,Evidence suggests the signal that PTP1B blocks insulin through making theinsulin receptor (IR) go for phosphorylation transfers to the route of leading.So any change of express competence and vigor about PTP1B which isrelated to IR may influence insulin signal transduction, and may cause theemergence of insulin impedance. So, for preventing and treatingⅡ-typediabetes and having positive function fatly to effective, specific inhibitor ofPTP1B.Obviously, Discovery for highly effective inhibitors of PTP1B has apromising application in diabetes and obesity therapy.Because of having tremendous flexility and favorable coordinatingcapabilities in synthesize, Schiff base metal complexes were broadlyregarded. They expressed many novel functions in biochemistry, medicineetc. Moreover, Peptides are important biomolecules, and have a veryimportant function in the living creature body. Dipetide Schiff basescontaining oxygen, nitrogen are bidentate and polydentate ligands. They aresimilar to bioactive molecules in the structure and property, and notpoisonous side effect. For possessing two kinds of coordination atoms, N andO, Dipetide Schiff base ligands have strongly capabilities coordinating tometal ions. In this paper, The interaction of dipetide Schiff base complexes and PTP 1B was studied. Detailed works mentioned below were carried out:1. Nine glycylglycine Schiff base complexes, VO(sal-glygly)·2H2O(1),Cd(sal-glygly)·1.5H2O(2), Mn(sal-glygly)·1.5H2O(3),[Mg(H2O)]6][CuL]2·4H2O(L=sal-glygly,4), [Nd(H2O)5(CuL)2][CuL]·8H2O(L=5-Brsal-glygly, 5), [La(H2O)5(CuL)2][CuL]·8H2O(L=5-Brsal-glygly,6),{[Ba(H2O)4(CuL)2]}n(L=sal-glygly,7), [Eu(H2O)5(NiL)2][NiL]·8H2O(L=5-Brsal-glygly,8),[Ba(NiL)2(H2O4]n (L=5-Brsal-glygly,9), weresynthesized and charactised by element analysis,IR spectrum, TG-DTAspectrum and X-ray and so on.2. The interaction of complexes 1-7 and alkaline phosphatase wasinvestigated. The results indicated that complexes 1 and 5 inhibited theactivity of the alkaline phosphatase in the experimental condition. IC50value of complex 1 to ALP was 1 x 10-4M with a mixed inhibition, its Kivalue being 52μM.3. The interaction of complexes and protein tyrosine phosphatase 1B wasalso investigated. The data indicated that complexes 1,6, 8 and 9 inhibitedthe activity of protein tyrosine phosphatase 1B in the experimentalcondition. IC50 value of complex 1 to PTP1B was 9×10-4M with a mixedinhibition, its Ki value being 60μM. |
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