|
Hypoglycemic activity of vanadyl complexes in recent years has become increasingly attention has been paid to its hypoglycemic mechanism is generally considered to be the combination of protein tyrosine phosphatase -1B (protein tyrosine phosphatase 1 B, PTP1B), competitive inhibition of PTP1B the activity achieve hypoglycemic effect . Six kinds of vanadyl complexes synthesized in this experiment , respectively, vanadyl oxalate (1) the oxalic peroxovanadate (2) , dihydrate malic acid the vanadyl (3 ) acetylacetonate, vanadyl (4) , acetylacetone - (8 - quinolinolato) the vanadyl (5) , 2 - (8 - quinolinolato) the vanadyl (6 ) . The complexes 5,6 have not been reported . By infrared spectroscopy , nuclear magnetic resonance , and differential thermal analysis of complex characterization to determine their structure . By UV spectroscopy tracking complexes 2,6 and reduced glutathione (GSH) interaction . Found that two complexes are reacted with GSH , and the resulting product is very stable . The experiments show that both sulfur - containing small molecule complexes with in vivo interactions, the binding sites may be a mercapto group of cysteine , provides certain experimental basis for the study of in vivo activity of the complexes , but the mechanism of action to be further experimental study . The studied complexes 2,4,5 and six pairs of protein tyrosine phosphatase -1B (PTP1B) inhibition vanadyl sulfate as a control , determination of the concentration of different complexes of PTP1B inhibition rate , tracking with objects of different concentrations of enzyme kinetics , get their IC50 values determine the inhibition type and inhibition mechanism was discussed .
|