Inhibition by Aplidine of the aggregation of the prion peptide PrP 106-126 into beta-sheet fibrils.
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.
Pérez
Mar
M
Centro de Biología Molecular, (CSIC/UAM) Facultad de Ciencias, Universidad Autónoma de Madrid, Canto Blanco, Madrid E28049, Spain.
Sadqi
Mourad
M
Muñoz
Victor
V
Avila
Jesús
J
D000818:Animals; D047630:Depsipeptides; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000378:metabolism* / Q000648:ultrastructure; D010456:Peptides, Cyclic / Q000378:metabolism*; D011328:Prions / Q000378:metabolism* / Q000648:ultrastructure; D020836:Protein Structure, Quaternary; D014561:Urochordata / Q000378:metabolism
D047630:Depsipeptides; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D011328:Prions; C082632:prion protein (106-126); C098980:plitidepsin