Thermoresponsive Controlled Association of Protein with a Dynamic Nanogel of Hydrophobized Polysaccharide and Cyclodextrin: Heat Shock Protein-Like Activity of Artificial Molecular Chaperone
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- 作者：Yuta Nomura ; Yoshihiro Sasaki ; Masaki Takagi ; Tadashi Narita ; Yasuhiro Aoyama ; and Kazunari Akiyoshi
- 刊名：Biomacromolecules
- 出版年：2005
- 出版时间：January 2005
- 年：2005
- 卷：6
- 期：1
- 页码：447 - 452
- 全文大小：193K
- 年卷期：v.6,no.1(January 2005)
- ISSN：1526-4602
文摘
Dynamic CHP-CD nanogels, which consisted of a self-assembly of cholesteryl-group-bearing pullulan (CHP)and 
-cyclodextrin (CD), were characterized by SEC and SEC-MALS methods. The nanogels preventedthe thermal aggregation of carbonic anhydrase B (CAB) by selective trapping of the heat-denatured protein.After the complex between the CHP-CD nanogels and CAB was cooled, the enzyme activity of CABspontaneously recovered upon release from the complex. The dynamic nanogels self-regulated an associationof heat denatured protein and dissociation of native protein depending on the concentration of CD. Thethermal stability of CAB was improved by thermoresponsive controlled association between the proteinsand the artificial molecular chaperone.
-cyclodextrin (CD), were characterized by SEC and SEC-MALS methods. The nanogels preventedthe thermal aggregation of carbonic anhydrase B (CAB) by selective trapping of the heat-denatured protein.After the complex between the CHP-CD nanogels and CAB was cooled, the enzyme activity of CABspontaneously recovered upon release from the complex. The dynamic nanogels self-regulated an associationof heat denatured protein and dissociation of native protein depending on the concentration of CD. Thethermal stability of CAB was improved by thermoresponsive controlled association between the proteinsand the artificial molecular chaperone.