Covalent and selective immobilization of GST fusion proteins with fluorophosphonate-based probes

Chem Commun (Camb). 2018 May 3;54(37):4661-4664. doi: 10.1039/c7cc08888d.

Abstract

Using GST fusion protein tags is an attractive approach for protein immobilization. Here we report that pyrimidine-based small-molecule probes with a fluorophosphonate reactive group could specifically react with the tyrosine-111 residue of the Schistosoma japonicum GST (sjGST) tag, and these probes could rapidly and site-selectively immobilize sjGST fusion proteins while preserving their activities.

MeSH terms

  • Animals
  • Glass / chemistry
  • Glutathione Transferase / chemistry*
  • Helminth Proteins / chemistry*
  • Humans
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / chemistry
  • Molecular Docking Simulation
  • Molecular Probes / chemical synthesis
  • Molecular Probes / chemistry*
  • Organofluorophosphonates / chemical synthesis
  • Organofluorophosphonates / chemistry*
  • Pyrimidines / chemical synthesis
  • Pyrimidines / chemistry
  • Recombinant Fusion Proteins / chemistry
  • Schistosoma japonicum / enzymology
  • Sepharose / chemistry
  • Tyrosine / chemistry

Substances

  • Helminth Proteins
  • Molecular Probes
  • Organofluorophosphonates
  • Pyrimidines
  • Recombinant Fusion Proteins
  • Tyrosine
  • Sepharose
  • Glutathione Transferase
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)