Photoreactive stapled BH3 peptides to dissect the BCL-2 family interactome

Craig R. Braun, Julian Mintseris, Evripidis Gavathiotis, Gregory H. Bird, Steven P. Gygi, Loren D. Walensky

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Defining protein interactions forms the basis for discovery of biological pathways, disease mechanisms, and opportunities for therapeutic intervention. To harness the robust binding affinity and selectivity of structured peptides for interactome discovery, we engineered photoreactive stapled BH3 peptide helices that covalently capture their physiologic BCL-2 family targets. The crosslinking α helices covalently trap both static and dynamic protein interactors, and enable rapid identification of interaction sites, providing a critical link between interactome discovery and targeted drug design.

Original languageEnglish (US)
Pages (from-to)1325-1333
Number of pages9
JournalChemistry and Biology
Volume17
Issue number12
DOIs
StatePublished - Dec 22 2010
Externally publishedYes

Fingerprint

Drug Design
Crosslinking
Proteins
Peptides
Pharmaceutical Preparations
Bax protein (53-86)
Therapeutics

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Molecular Biology
  • Clinical Biochemistry
  • Molecular Medicine
  • Pharmacology

Cite this

Photoreactive stapled BH3 peptides to dissect the BCL-2 family interactome. / Braun, Craig R.; Mintseris, Julian; Gavathiotis, Evripidis; Bird, Gregory H.; Gygi, Steven P.; Walensky, Loren D.

In: Chemistry and Biology, Vol. 17, No. 12, 22.12.2010, p. 1325-1333.

Research output: Contribution to journalArticle

Braun, Craig R. ; Mintseris, Julian ; Gavathiotis, Evripidis ; Bird, Gregory H. ; Gygi, Steven P. ; Walensky, Loren D. / Photoreactive stapled BH3 peptides to dissect the BCL-2 family interactome. In: Chemistry and Biology. 2010 ; Vol. 17, No. 12. pp. 1325-1333.
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