Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs

Shinichi Sato, Hiroshi Aoyama, Hiroyuki Miyachi, Mikihiko Naito, Yuichi Hashimoto

Research output: Contribution to journalArticle

19 Citations (Scopus)


Overexpression of cIAP1 correlates with resistance to radiotherapy and chemotherapy in various cancers. Recently, we reported that a class of bestatin ester analogs represented by MeBS (2) destabilized and promoted the degradation of cIAP1 through auto-ubiquitination, and thereby sensitized cancer cells to apoptosis. Herein, we present chemical evidence that bestatin ester analogs directly interact with the cIAP1-BIR3 domain by means of fluorescence polarization assay and photoaffinity labeling assay using fluorescent probes.

Original languageEnglish
Pages (from-to)3354-3358
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Issue number11
Publication statusPublished - Jun 1 2008
Externally publishedYes



  • Bestatin
  • BIR3 domain
  • cIAP1
  • Fluorescence polarization
  • Photoaffinity labeling

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

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