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Protein folding, misfolding, and refolding of therapeutic proteins

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Abstract

Substantial progress has been made towards understanding the folding mechanisms of proteins in vitro and in vivo even though the general rules governing such folding events remain unknown. This paper reviews current folding models along with experimental approaches used to elucidate the folding pathways. Protein misfolding is discussed in relation to disease states, such as amyloidosis, and the recent findings on the mechanism of converting normally soluble proteins into amyloid fibrils through the formation of intermediates provide an insight into understanding the pathogenesis of amyloid formation and possible clues for the development of therapeutic treatments. Finally, some commonly adopted refolding strategies developed over the past decade are summarized.

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  1. Department of Bioinformatics and Life Science, Soongsil University, 156-743, Seoul, Korea

    Hang-Cheol Shin

  2. Bioproducts Research Center, Yonsei University, 120-749, Seoul, Korea

    Hang-Cheol Shin

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Shin, HC. Protein folding, misfolding, and refolding of therapeutic proteins. Biotechnol. Bioprocess Eng. 6, 237–243 (2001). https://doi.org/10.1007/BF02931984

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