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Journal of Biochemistry Advance Access published online on November 26, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm224
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© 2007 The Japanese Biochemical Society

Copper(II) Inhibits in Vitro Conformational Conversion of Ovine Prion Protein Triggered by Low pH

Mei-li Liu1, Yu-xing Li2, Xiang-mei Zhou1 and De-ming Zhao1,*

1 National Animal TSE Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing 100094, China
2 Vaccine Research Center,National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.

*Address correspondence and reprint requests to: Deming Zhao, College of Veterinary Medicine, China Agricultural University, Haidian District Yuanmingyuan Xi Lu 2, Beijing 100094, China. TEL & FAX: +86-10-62732975. E-mail: zhaodm{at}cau.edu.cn

Received August 22, 2007; Accepted November 12, 2007


  Abstract

To gain insight into the conformational conversion of ovine prion protein (OvPrPC) at different pH values and/or in the presence of CuCl2, the secondary structure of OvPrPC was analyzed by circular dichroism (CD) spectroscopy. Copper treatment of OvPrPC under moderately acidic conditions (pH 5.0~6.0) as well as physiological conditions (pH 7.4) also makes OvPrPC adopt protease-resistant and β-sheet rich conformation. However, under lower pH conditions (2.0~4.5) with copper treatment, OvPrPC gained higher {alpha}-helix structure. This study demonstrated that Cu2+ can significantly modulate conformational conversion triggered by acidic pH, and this will provide therapeutic intervention approaches for prion diseases.

Key Words: Circular dichroism spectra (CD), Conformational conversion, Copper, Ovine Prion protein, pH, Protease K


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