Surface Plasmon Resonance Analysis for the Screening of Anti-prion Compounds
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概要
- 論文の詳細を見る
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.
- 公益社団法人日本薬学会の論文
- 2006-05-01
著者
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Iwaki Toru
Department Of Materials Science Graduate School Of Engineering Tohoku University
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Iwaki Toru
Department Of Neuropathology Neurological Institute Kyushu University
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Nishimura Yuki
Department Of Cardiovascular And Renal Medicine Saga University Faculty Of Medicine
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Nishimura Yuki
Department Of Prion Research Tohoku University
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Doh-ura Katsumi
Departmenr Of Neuropathology Neurological Institute Graduate School Of Medical Sciences Kyushu Unive
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SAKAGUCHI Suehiro
Department of Molecular Microbiology and Immunology, Nagasaki University, Graduate School of Biomedi
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Doh-ura Katsumi
Department Of Prion Research Tohoku University
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Kawatake Satoshi
Department Of Prion Research Tohoku University
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Sakaguchi Suehiro
Department Of Molecular Microbiology And Immunology Nagasaki University
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Iwaki Toru
Department of Chemistry, Faculty of Science, Hiroshima University
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