BioMetals

, Volume 23, Issue 6, pp 1139–1147

Inhibition protein tyrosine phosphatases by an oxovanadium glutamate complex, Na2[VO(Glu)2(CH3OH)](Glu = glutamate)

Article

Abstract

The insulin-sensitizing effect of vanadium complexes has been linked to their ability to inhibit protein tyrosine phosphatases (PTPs). Considering that vanadium complexes may exchange in vivo with amino acids, forming in situ vanadium–amino acid complexes, we have synthesized and characterized an oxovanadium glutamate complex, Na2[V(IV)O(Glu)2(CH3OH)]H2O (1·H2O). The complex showed potent inhibition against four human PTPs (PTP1B, TCPTP, HePTP, and SHP-1) with IC50 in the 0.21–0.37 μM ranges. Fluorescence titration studies suggest that the complex binds to PTP1B with the formation of a 2:1 complex. Enzyme kinetics analysis using Lineweaver–Burk plots indicates a typical competitive inhibition mode.

Keywords

Protein tyrosine phosphatases Inhibition Oxovanadium–glutamate complex Fluorescence 

Copyright information

© Springer Science+Business Media, LLC. 2010

Authors and Affiliations

  1. 1.Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of the Education MinistryShanxi UniversityTaiyuanPeople’s Republic of China
  2. 2.Department of Chemistry and BiochemistryUniversity of MassachusettsDartmouthUSA
  3. 3.Edmond H. Fischer Signal Transduction LaboratoryCollege of Life Sciences, Jilin UniversityChangchunPeople’s Republic of China
  4. 4.State Key Laboratory of Coordination ChemistryNanjing UniversityNanjingPeople’s Republic of China

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