Inhibition by aplidine of the aggregation of the prion peptide PrP 106-126 into β-sheet fibrils

[摘要] Aplidine, a cyclic peptide, from the tunicate Aplidium albican, prevents the in vitro aggregation into beta-sheet containing fibrils of the prion peptide 106-126 when co-incubated in a 1: 1 molar ratio. The blocking of fibril formation induced by Aplidine has clear sequence specificity, being much stronger for the 106-126 prion peptide than for the beta-amyloid 25-35 peptide. In addition to the known ability of Aplidine to cross the plasmatic membrane, these results indicate that Aplidine is a potential leading compound for the development of therapeutic blockers of prion aggregation. (C) 2003 Elsevier B.V. All rights reserved.

[发布日期] 2003-10-15

[关键词] aplidine;prion peptide;inhibition of aggregation