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Chemical Chaperone and Inhibitor Discovery: Potential Treatments for Protein Conformational Diseases

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Author(s): Jian-Hua Zhao | Hsuan-Liang Liu | Hsin-Yi Lin | Chih-Hung Huang | Hsu-Wei Fang | Shiao-Shing Chen | Yih Ho | Wei-Bor Tsai | Wen-Yih Chen

Journal: Perspectives in Medicinal Chemistry
ISSN 1177-391X

Volume: 2007;
Issue: 1;
Start page: 39;
Date: 2007;
Original page

ABSTRACT
Protein misfolding and aggregation cause a large number of neurodegenerative diseases in humans due to (i) gain of function as observed in Alzheimer’s disease, Huntington’s disease, Parkinson’s disease, and Prion’s disease or (ii) loss of function as observed in cystic fi brosis and α1-antitrypsin defi ciency. These misfolded proteins could either lead to the formation of harmful amyloids that become toxic for the cells or to be recognized and prematurely degraded by the protein quality control system. An increasing number of studies has indicated that some low-molecular-weight compounds named as chemical chaperones can reverse the mislocalization and/or aggregation of proteins associated with human conformational diseases. These small molecules are thought to non-selectively stabilize proteins and facilitate their folding. In this review, we summarize the probable mechanisms of protein conformational diseases in humans and the use of chemical chaperones and inhibitors as potential therapeutic agents against these diseases. Furthermore, recent advanced experimental and theoretical approaches underlying the detailed mechanisms of protein conformational changes and current structure-based drug designs towards protein conformational diseases are also discussed. It is believed that a better understanding of the mechanisms of conformational changes as well as the biological functions of these proteins will lead to the development and design of potential interfering compounds against amyloid formation associated with protein conformational diseases.
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