NR AUUB
AU Kawatake,S.; Nishimura,Y.; Sakaguchi,S.; Iwaki,T.; Doh-ura,K.
TI Surface plasmon resonance analysis for the screening of anti-prion compounds
QU Biological and Pharmaceutical Bulletin 2006 May; 29(5): 927-32
PT journal article
AB 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.
MH Animals; Anti-Infective Agents/*pharmacology; Antimalarials/pharmacology; Cell Line; Drug Evaluation, Preclinical; Kinetics; Mice; Prions/antagonists & inhibitors/*drug effects; Protein Binding; Recombinant Proteins/antagonists & inhibitors; Research Support, Non-U.S. Gov't; Scrapie/pathology; Surface Plasmon Resonance
AD Department of Prion Research, Tohoku University, Sendai, Japan.
SP englisch
PO Japan