Development of molecular probes for second-site screening and design of protein tyrosine phosphatase inhibitors

J Med Chem. 2007 May 3;50(9):2137-43. doi: 10.1021/jm061481l. Epub 2007 Mar 30.

Abstract

We report on the design, synthesis, and evaluation of a series of furanyl-salicyl-nitroxide derivatives as effective chemical probes for second-site screening against phosphotyrosine phosphatases (PTPs) using NMR-based techniques. The compounds have been tested against a panel of PTPs to assess their ability to inhibit a broad spectrum of these phosphatases. The utility of the derived compounds is illustrated with the phosphatase YopH, a bacterial toxin from Yersinia pestis. Novel chemical fragments were identified during an NMR-based screen for compounds that are capable of binding on the surface of YopH in regions adjacent the catalytic site in the presence of the spin-labeled compounds. Our data demonstrate the value of the derived chemical probes for NMR-based second-site screening in PTPs.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Outer Membrane Proteins / antagonists & inhibitors*
  • Bacterial Outer Membrane Proteins / chemistry*
  • Catalytic Domain
  • Cyclic N-Oxides / chemical synthesis*
  • Cyclic N-Oxides / chemistry
  • Furans / chemical synthesis*
  • Furans / chemistry
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*
  • Protein Tyrosine Phosphatases / chemistry*
  • Salicylates / chemical synthesis*
  • Salicylates / chemistry
  • Spin Labels / chemical synthesis*
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Bacterial Outer Membrane Proteins
  • Cyclic N-Oxides
  • Furans
  • Salicylates
  • Spin Labels
  • Protein Tyrosine Phosphatases
  • yopH protein, Yersinia