Surface Plasmon Resonance Analysis for the Screening of Anti-prion Compounds

作者：Satoshi Kawatake, Yuki Nishimura, Suehiro Sakaguchi, Toru Iwaki, Katsumi Doh‐ura · 发表于：Biological and Pharmaceutical Bulletin · 年份：2006 · DOI：10.1248/bpb.29.927 · 被引用次数：47 · 研究领域：Prion Diseases and Protein Misfolding、Trace Elements in Health、Monoclonal and Polyclonal Antibodies Research

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.