NR APKU
AU Perez,M.; Sadqi,M.; Munoz,V.; Avila,J.
TI Inhibition by Aplidine of the aggregation of the prion peptide PrP 106-126 into beta-sheet fibrils
QU Biochimica et Biophysica Acta 2003 Oct 15; 1639(2): 133-9
PT journal article
AB 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.
MH Animals; Microscopy, Electron; Peptide Fragments/*metabolism/ultrastructure; Peptides, Cyclic/*metabolism; Prions/*metabolism/ultrastructure; *Protein Structure, Quaternary; Support, Non-U.S. Gov't; Urochordata/metabolism
AD Centro de Biologia Molecular, (CSIC/UAM) Facultad de Ciencias, Universidad Autonoma de Madrid, Canto Blanco, Madrid E28049, Spain.
SP englisch
PO Niederlande