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Protein refolding assisted by self‐assembled nanogels as novel artificial molecular chaperone
Author(s) -
Nomura Yuta,
Ikeda Masahiro,
Yamaguchi Nozomi,
Aoyama Yasuhiro,
Akiyoshi Kazunari
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01028-7
Subject(s) - nanogel , chemistry , chaperone (clinical) , carbonic anhydrase , serine protease , biochemistry , denaturation (fissile materials) , chaotropic agent , biophysics , enzyme , protease , drug delivery , biology , organic chemistry , medicine , pathology , nuclear chemistry
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.