Peptidyl aldehydes as slow-binding inhibitors of dual-specificity phosphatases

Bioorg Med Chem Lett. 2004 Feb 9;14(3):685-7. doi: 10.1016/j.bmcl.2003.11.027.

Abstract

Peptidyl aldehydes were tested for inhibition of dual-specificity phosphatases VH1 and VHR. The most potent compound, cinnamaldehyde-Gly-Glu-Glu (Cinn-GEE), acted as a slow-binding inhibitor with K(I)* values of 18 and 288 microM against VH1 and VHR, respectively.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acrolein / analogs & derivatives*
  • Acrolein / chemistry
  • Acrolein / metabolism*
  • Acrolein / pharmacology*
  • Antineoplastic Agents, Phytogenic / chemistry
  • Antineoplastic Agents, Phytogenic / metabolism*
  • Antineoplastic Agents, Phytogenic / pharmacology*
  • Binding Sites
  • Dual Specificity Phosphatase 3
  • Dual-Specificity Phosphatases
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Peptide Fragments / pharmacology*
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*
  • Protein Tyrosine Phosphatases / metabolism

Substances

  • Antineoplastic Agents, Phytogenic
  • Enzyme Inhibitors
  • Peptide Fragments
  • Acrolein
  • dual specificity phosphatase 12
  • DUSP3 protein, human
  • Dual Specificity Phosphatase 3
  • Dual-Specificity Phosphatases
  • Protein Tyrosine Phosphatases
  • cinnamaldehyde