Periodate-triggered cross-linking of DOPA-containing peptide-protein complexes

Lyle Burdine, Thomas G. Gillette, Hai Jun Lin, Thomas Kodadek

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

Chemical cross-linking is a powerful methodology for analyzing proteins-small molecule and protein-protein interactions. We describe the development of a new chemical cross-linking reaction for the study of protein complexes. Specifically, we show that molecules containing an ortho dihydroxyarene unit can be oxidized selectively with sodium periodate in the presence of native proteins, producing an ortho quinone intermediate that can cross-link with suitable nearby protein residues. We demonstrate the efficacy and specificity of this chemistry for a peptide-protein complex and also deduce the binding site of an artificial activation domain on a proteasome subcomplex.

Original languageEnglish (US)
Pages (from-to)11442-11443
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number37
DOIs
StatePublished - Sep 22 2004

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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