Thermoresponsive controlled association of protein with a dynamic nanogel of hydrophobized polysaccharide and cyclodextrin: Heat shock protein-like activity of artificial molecular chaperone

被引：88

作者：

Nomura, Y

Sasaki, Y

Takagi, M

Narita, T

Aoyama, Y

Akiyoshi, K

机构：

[1] Tokyo Med & Dent Univ, Inst Biomat & Bioengn, Chiyoda Ku, Tokyo 1010062, Japan

[2] Tokyo Med & Dent Univ, Ctr Excellence, Program Frontier Res Mol Destruct & Reconstruct T, Tokyo 1010062, Japan

[3] Kyoto Univ, Grad Sch Engn, Dept Synthet Chem & Biol Chem, Sakyo Ku, Kyoto 6068501, Japan

[4] Saitama Inst Technol, Grad Sch Engn, Dept Mat Sci & Engn, Okabe, Saitama 3690293, Japan

来源：

BIOMACROMOLECULES | 2005年 / 6卷 / 01期

关键词：

D O I：

10.1021/bm049501t

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Dynamic CHP-CD nanogels, which consisted of a self-assembly of cholesteryl-group-bearing pullulan (CHP) and beta-cyclodextrin (CD), were characterized by SEC and SEC-MALS methods. The nanogels prevented the 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 CAB spontaneously recovered upon release from the complex. The dynamic nanogels self-regulated an association of heat denatured protein and dissociation of native protein depending on the concentration of CD. The thermal stability of CAB was improved by thermoresponsive controlled association between the proteins and the artificial molecular chaperone.

引用

页码：447 / 452

页数：6

共 31 条

[1] Molecular chaperone-like activity of hydrogel nanoparticles of hydrophobized pullulan: Thermal stabilization with refolding of carbonic anhydrase B [J].