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Journal of Biochemistry Advance Access originally published online on November 26, 2007
Journal of Biochemistry 2008 143(3):333-337; 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,*

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

*To whom correspondence should be addressed. Tel: +86 10 62732975, 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 analysed 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, conformational conversion, copper, ovine prion protein, pH, protease K

Abbreviations: BSE, bovine spongiform encephalopathy; CD, circular dichroism; OvPrPC, ovine prion protein; PK, protease K ovine prion; PrP, prion protein; TSE, transmissible spongiform encephalopathies


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