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

Abstract

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.

Keywords: :

• brain-peptide libraries
• conformational change
• de novo designed peptide
• recombinant bovine prion protein
• synaptophysin

10.4161/pri.27961

Disclosure of Potential Conflicts of Interest

No potential conflicts of interest were disclosed.

Acknowledgments

Authors thanks to Drs K Kasai, T Yokoyama and S Mohri, National Institute for Animal Health for variable discussions and Dr V Wray, Helmholtz Centre for Infection Research, Braunschweig, Germany, for linguistic advice. A part of this work was funded by the Research and Development Program for New Bio-industry Initiatives, National Agriculture and Food Research Organization (2007–2011).