Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions.
Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions.
复制标题
拥挤环境中渗透剂对蛋白质-溶剂相互作用的影响：分析拥挤溶液中 TMAO 对蛋白质的影响。
DOI：
10.1016/j.abb.2015.02.021
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发表时间：
2015
影响因子：
3.9
通讯作者：
Uversky,VladimirN
中科院分区：
文献类型：
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作者：
Breydo,Leonid;Sales,AmandaE;Ferreira,Luisa;Fedotoff,Olga;Shevelyova,MarinaP;Permyakov,SergeiE;Kroeck,KyleG;Permyakov,EugeneA;Zaslavsky,BorisY;Uversky,VladimirN
我们分析了天然渗透剂，三甲胺N-氧化物（TMAO），在大分子拥挤条件下的几种蛋白质的结构特性和构象稳定性的影响，由一组生物物理技术。我们还使用了溶剂相互作用分析方法来研究拥挤条件下TMAO-蛋白质相互作用的特殊性。为此，我们分析了这些蛋白质在无TMAO和含TMAO的双水相系统（ATPS）中的分配。这些ATPS具有6.0重量%的相同聚合物组成，PEG-8000和12.0重量%葡聚糖-75和相同离子组成的0.01 M K/NaPB，pH 7.4。这些分析表明，TMAO与蛋白质没有直接的相互作用，表明TMAO对拥挤溶液中蛋白质结构的影响是通过这种渗透剂对水介质溶剂性质的影响而发生的。在聚合物存在下，TMAO对蛋白质结构的影响是相当复杂和蛋白质特异性的。奇怪的是，我们的研究表明，在高浓度的聚合物溶液中，TMAO并不总是促进蛋白质的进一步折叠。
We analyzed the effect of a natural osmolyte, trimethylamine N-oxide (TMAO), on structural properties and conformational stabilities of several proteins under macromolecular crowding conditions by a set of biophysical techniques. We also used the solvent interaction analysis method to look at the peculiarities of the TMAO-protein interactions under crowded conditions. To this end, we analyzed the partitioning of these proteins in TMAO-free and TMAO-containing aqueous two-phase systems (ATPSs). These ATPSs had the same polymer composition of 6.0 wt.% PEG-8000 and 12.0 wt.% dextran-75, and same ionic composition of 0.01 M K/NaPB, pH 7.4. These analyses revealed that there is no direct interaction of TMAO with proteins, suggesting that the TMAO effects on the protein structure in crowded solutions occur via the effects of this osmolyte on solvent properties of aqueous media. The effects of TMAO on protein structure in the presence of polymers were rather complex and protein-specific. Curiously, our study revealed that in highly concentrated polymer solutions, TMAO does not always act to promote further protein folding.