15 フェオフィチン類の異常型プリオンタンパク質複製阻害機構の解明(口頭発表の部)

概要

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Prion diseases, also known as transmissible spongiform encephalopathies, are believed to be caused by accumulation of an abnormal isoform of the prion protein (PrP^<Sc>) in the central nervous system. The proposed replicative cycle of prion is relatively simple. It encompasses misfolding of a single protein, the cellular prion protein (PrP^C) into PrP^<Sc>. The problem is that there is no significant effective medicine for these diseases. Therefore we planned to search for new effective compounds from natural resources using competitive ELISA. In consequence, pheophytin a (Phe-a), which has high-affinity to PrP^C was found from a medicinal plant, Conandron ramondiodes, and a brown algae Ecklonia kurome. Further investigation clarified that Phe-a inhibits the formation of PrP^<Sc> in prion-infected neuroblastoma cells (ScN2a and F3). This finding suggest that Phe-a might be useful for the prevention of prion diseases, but a mechanism to inhibit the prion replication is still unknown. Then we investigated the interactive analysis of prion and Phe-a using some spectroscopic methods(CD and NMR spectra). As a result, it revealed that one mole of Phe-a binds to the second α-helix of PrP^C 121-231, and stabilizes its conformation.
天然有機化合物討論会の論文
2007-08-24