Model investigations for vanadium-protein interactions: Synthesis, characterization and antidiabetic properties

Abstract Reaction of NNO donor Schiff bases with vanadyl sulphate afforded the complexes viz ., [VO(L 1 )(H 2 O)]NO 3 1 , [VO(L 2 )(H 2 O)]NO 3 2 , [VO(L 2 )(ImH) 2 ]SO 4 ·H 2 O 3 and [VO(L 1 )ImH]NO 3 4 (where, L 1  = Acetic acid (2-hydroxy-3-methoxy-benzylidene)-hydrazide and L 2  = 5-bromo-2-[(E)-(pyridine-2-ylhydrazono)methyl]phenol). In complex 3 the oxidation state of vanadium was found to be +5, while in rest all complexes it was +4. The crystal structure of complex 3 was solved by single crystal X-ray analysis. In addition to synthesis, optical, infrared and electrochemical properties of these complexes were also carried out. Electron paramagnetic spectra of oxidovanadium(IV/V) complexes is reported as well. Docking experiments were performed to study the molecular binding behaviour of all complexes with α-glucosidase enzyme. An antidiabetic feature like α-amylase and α-glucosidase inhibition studies made them promising candidates as inhibitors of insulin enzyme.