Protein refolding assisted by self‐assembled nanogels as novel artificial molecular chaperone

FEBS Letters

Aoyama, Yasuhiro²  Yamaguchi, Nozomi³  Akiyoshi, Kazunari¹  Ikeda, Masahiro²  Nomura, Yuta² 

[1] Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kannda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan;Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Yoshida-Hommachi, Sakyo-ku, Kyoto 606-8501, Japan;Department of Cell Biology, Research Institute for Neurological Diseases and Geriatrics, Kyoto Prefectural University of Medicine, Kawaramachi-Hirokoji, Kyoto 602-8566, Japan

关键词: Artificial chaperone;    Protein refolding;    Inclusion body;    Hydrophobized polysaccharide;    Cyclodextrin;    Nanogel;   

DOI  :  10.1016/S0014-5793(03)01028-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Molecular chaperone-like activity for protein refolding was investigated using nanogels of self-assembly of cholesterol-bearing pullulan. Nanogels effectively prevented protein aggregation (i.e. carbonic anhydrase and citrate synthase) during protein refolding from GdmCl denaturation. Enzyme activity recovered in high yields upon dissociation of the gel structure in which the proteins were trapped, by the addition of cyclodextrins. The nanogels assisted protein refolding in a manner similar to the mechanism of molecular chaperones, namely by catching and releasing proteins. The nanogels acted as a host for the trapping of refolded intermediate proteins. Cyclodextrin is an effector molecule that controls the binding ability of these host nanogels to proteins. The present nanogel system was also effective at the renaturation of inclusion body of a recombinant protein of the serine protease family.

【 授权许可】

Unknown