Inhibition by Aplidine of the aggregation of the prion peptide PrP 106-126 into beta-sheet fibrils.

  title={Inhibition by Aplidine of the aggregation of the prion peptide PrP 106-126 into beta-sheet fibrils.},
  author={M. P{\'e}rez and M. Sadqi and V. Mu{\~n}oz and J. {\'A}vila},
  journal={Biochimica et biophysica acta},
  volume={1639 2},
  • M. Pérez, M. Sadqi, +1 author J. Ávila
  • Published 2003
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 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… CONTINUE READING
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