NR AXZH
AU Yang,J.; Liu,M.; Zhao,D.
TI Copper(II) Inhibits in Vitro Conformational Conversion of Ovine Prion Protein Triggered by Low pH
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Protein Misfolding P01.50
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB
Background: One of the critical events in the pathogenesis of transmissible spongiform encephalopathies (prion diseases) is the conversion of a cellular prion protein (PrPc) into a protease-resistant, ß-sheet rich isoform (PrPsc). Under certain conditions, prion protein (PrP) undergoes a conformational change from PrPc to PrPsc.
Aim: It is to gain insight into the conformational conversion of ovine prion protein PrP23-256(OvPrP23-256) at various pH and/or in the presence of copper (2) chloride (CuCl2).
Methods:Secondary structure of recombinant OvPrP23-256 with scrapie susceptible ARQ genotype was analyzed by circular dichroism (CD) spectrum.
Results: In consistent with other previous studies, acidic pH triggers the formation of protease-resistant and ß-sheet rich isoform of OvPrP23-256. Copper treatment of OvPrP23-256 at moderate acidic condition pH 5.0-6.0 as well as physiological condition (pH 7.4) also makes OvPrP23-256 adopt protease-resistant and ß-sheet rich conformation. However, at lower pH condition (2.0-4.5) with copper treatment, OvPrP23-256 possessed more a-helix content with low ß-sheet.
Discussion and Conclusion: Together, the study demonstrated that Cu2+ can drastically modulate conformational conversion triggered by acidic pH condition in OvPrP23-256, which possesses protease resistance and ß-sheet rich phenotype. These results provide new insight into the prion protein conformational conversion process.
AD J. Yang, M. Liu, D. Zhao, China Agricultural University, College of Veterinary Medicine, China
SP englisch
PO Schottland