Surface plasmon resonance analysis for the screening of anti-prion compounds.
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.
Kawatake
Satoshi
S
Department of Prion Research, Tohoku University, Sendai, Japan.
Nishimura
Yuki
Y
Sakaguchi
Suehiro
S
Iwaki
Toru
T
Doh-ura
Katsumi
K
D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology*; D000962:Antimalarials / Q000494:pharmacology; D002460:Cell Line; D004353:Drug Evaluation, Preclinical; D007700:Kinetics; D051379:Mice; D011328:Prions / Q000037:antagonists & inhibitors / Q000187:drug effects*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors; D012608:Scrapie / Q000473:pathology; D020349:Surface Plasmon Resonance
D000890:Anti-Infective Agents; D000962:Antimalarials; D011328:Prions; D011994:Recombinant Proteins