Surface plasmon resonance analysis for the screening of anti-prion compounds

Satoshi Kawatake, Yuki Nishimura, Suehiro Sakaguchi, Toru Iwaki, Katsumi Doh-Ura

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The interaction of anti-prion compounds and amyloid binding dyes with a carboxy-terminal domain of prion protein (PrP121-231) was examined using surface plasmon resonance (SPR) and compared with inhibition activities of abnormal PrP formation in scrapie-infected cells. Most examined compounds had affinities for PrP121-231: antimalarials had low affinities, whereas Congo red, phthalocyanine and thioflavin S had high affinities. The SPR binding response correlated with the inhibition activity of abnormal PrP formation. Several drugs were screened using SPR to verify the findings: propranolol was identified as a new anti-prion compound. This fact indicates that drug screenings by this assay are useful.

Original languageEnglish
Pages (from-to)927-932
Number of pages6
JournalBiological and Pharmaceutical Bulletin
Issue number5
Publication statusPublished - May 1 2006


All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science

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