Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
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DOI：
10.1016/s0014-5793(03)01028-7
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发表时间：
2003-10-23
期刊：
影响因子：
3.5
通讯作者：
Akiyoshi, K
中科院分区：
文献类型：
--
作者：
Nomura, Y;Ikeda, M;Akiyoshi, K
利用含胆固醇的普鲁兰多糖自组装纳米凝胶研究了蛋白质重折叠的分子伴侣样活性。纳米凝胶有效地防止蛋白质聚集（即碳酸酐酶和柠檬酸合酶）在蛋白质重折叠从GdmCl变性。通过加入环糊精，在蛋白质被捕获的凝胶结构解离后，酶活性以高产率恢复。纳米凝胶以类似于分子伴侣机制的方式辅助蛋白质重折叠，即通过捕获和释放蛋白质。纳米凝胶充当了捕获重折叠中间蛋白质的宿主。环糊精是控制这些宿主纳米凝胶与蛋白质结合能力的效应分子。本发明的纳米凝胶系统在丝氨酸蛋白酶家族的重组蛋白的包涵体的复性中也是有效的。(C)2003年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.