Disparate proteome reactivity profiles of carbon electrophiles

Nat Chem Biol. 2008 Jul;4(7):405-7. doi: 10.1038/nchembio.91. Epub 2008 May 18.


Insights into the proteome reactivity of electrophiles are crucial for designing activity-based probes for enzymes lacking cognate affinity labels. Here, we show that different classes of carbon electrophiles exhibit markedly distinct amino acid labeling profiles in proteomes, ranging from selective reactivity with cysteine to adducts with several amino acids. These data specify electrophilic chemotypes with restricted and permissive reactivity profiles to guide the design of next-generation functional proteomics probes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Cysteine Endopeptidases / chemistry*
  • Molecular Probes / chemistry*
  • Proteome / chemistry*
  • Proteomics / methods*
  • Sensitivity and Specificity
  • Serine Endopeptidases / chemistry*
  • Structure-Activity Relationship


  • Amino Acids
  • Molecular Probes
  • Proteome
  • Serine Endopeptidases
  • Cysteine Endopeptidases

Associated data

  • PubChem-Substance/49699415
  • PubChem-Substance/49699416
  • PubChem-Substance/49699417
  • PubChem-Substance/49699418
  • PubChem-Substance/49699419