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

• Published in: Biological & Pharmaceutical Bulletin Vol. 29; no. 5; pp. 927 - 932
• Main Authors: Kawatake, Satoshi, Nishimura, Yuki, Sakaguchi, Suehiro, Iwaki, Toru, Doh-ura, Katsumi
• Format: Journal Article
• Language: English
• Published: Japan The Pharmaceutical Society of Japan 01.05.2006; Pharmaceutical Society of Japan; Japan Science and Technology Agency
• Subjects: Animals; Anti-Infective Agents - pharmacology; anti-prion compound; Antimalarials - pharmacology; Cell Line; Drug Evaluation, Preclinical; Kinetics; Mice; Prions - antagonists & inhibitors; Prions - drug effects; Protein Binding; recombinant prion protein; Recombinant Proteins - antagonists & inhibitors; Scrapie - pathology; scrapie-infected cell; screening; Surface Plasmon Resonance
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.29.927

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.