Label transfer chemistry for the characterization of protein-protein interactions

Bo Liu, Chase T. Archer, Lyle Burdine, Thomas G. Gillette, Thomas Kodadek

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


A new label transfer method is presented that overcomes most of the limitations of current systems. A protein of interest is tagged with a tetracysteine sequence (FlAsH receptor peptide (FRP)) that binds tightly and specifically to a chimeric molecule 3,4-dihydroxyphenylalanine-biotin-4′,5′-bis(1,3,2-dithioarsolan-2-yl)fluorescein (DOPA-biotin-FlAsH). Upon brief periodate oxidation, the DOPA moiety is cross-linked to nearby surface-exposed nucleophiles. Boiling the products in excess dithiol dissolves the FlAsH-FRP interaction, resulting in transfer of the biotin tag to the partner proteins, allowingthem to be identified by standard methods.

Original languageEnglish (US)
Pages (from-to)12348-12349
Number of pages2
JournalJournal of the American Chemical Society
Issue number41
StatePublished - Oct 17 2007

ASJC Scopus subject areas

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


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