Catalysis of oxidative protein folding by small-molecule diselenides
Catalysis of oxidative protein folding by small-molecule diselenides
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DOI：
10.1021/bi8008906
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发表时间：
2008-07-08
期刊：
影响因子：
2.9
通讯作者：
Hilvert, Donald
中科院分区：
文献类型：
--
作者：
Beld, Joris;Woycechowsky, Kenneth J.;Hilvert, Donald
含有二硫键的重组蛋白质的生产通常需要在体外进行氧化折叠。在这里，我们证明了二硒醚，如硒谷胱甘肽，催化O(2)的氧化蛋白质折叠。因此，由硒谷胱甘肽和谷胱甘肽的硫醇形式组成的氧化还原缓冲液的浓度大大降低，可以获得与标准谷胱甘肽氧化还原缓冲液相同的折叠速度和产率。此外，硒醇的低pK(A)将硒谷胱甘肽折叠的pH范围扩展到谷胱甘肽不活跃的酸性条件。因此，利用二硒醚的催化能力可能会为更有效的氧化蛋白质折叠铺平道路。
The production of recombinant, disulfide-containing proteins often requires oxidative folding in vitro. Here, we show that diselenides, such as selenoglutathione, catalyze oxidative protein folding by O(2). Substantially lower concentrations of a redox buffer composed of selenoglutathione and the thiol form of glutathione can consequently be used to achieve the same rate and yield of folding as a standard glutathione redox buffer. Further, the low pK(a) of selenols extends the pH range for folding by selenoglutathione to acidic conditions, where glutathione is inactive. Harnessing the catalytic power of diselenides may thus pave the way for more efficient oxidative protein folding.