Disulfide bonds in amyloidogenesis diseases related proteins

Authors

  • Yang Li,

    1. Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China
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  • Juan Yan,

    1. Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China
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  • Xin Zhang,

    1. Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China
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  • Kun Huang

    Corresponding author
    1. Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China
    2. Centre for Biomedicine Research, Wuhan Institute of Biotechnology, Wuhan, Hubei, People's Republic of China
    • Correspondence to: Kun Huang, Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, China, 430030. E-mail: kunhuang2008@hotmail.com

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ABSTRACT

More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and prion disease, originate from the deposition of misfolded proteins. These proteins, referred as amyloidogenic proteins, adopt a β-sheet-rich structure when transformed from soluble state into insoluble amyloid fibrils. Amyloid formation is influenced by a number of factors that affect the intermolecular interaction, including pH, temperature, ion strength, and chemical bonds. In this review, we focus on the role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidogenic proteins. The effects of introduced disulfide bonds on the amyloidogenicity of proteins lacking native disulfide are also reviewed. Proteins 2013; 81:1862–1873. © 2013 Wiley Periodicals, Inc.

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