Design and syntheses of peptides which induce or enhance structural changes of recombinant bovine prion protein (rbPrP) and discovery of peptides from bovine brain which accelerate structural conversions of rbPrP

摘要

The co-existence of certain peptides influenced the kinetic rate of aggregation and the lag-time of fibril formation of rbPrP. Using recently developed structural conversion assay system, peptides have been screened from bovine brain peptide library. Peptide sequences of positive components have been elucidated by mass spectrometry and chemically synthesized to confirm actions.