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Kawatake, Satoshi; Nishimura, Yuki; Sakaguchi, Suehiro; Iwaki, Toru; Doh-ura, Katsumi
Biological & Pharmaceutical Bulletin, 05/2006, Volume: 29, Issue: 5Journal Article
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.
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