Effects of sodium dodecyl sulfate, Sarkosyl and sodium lauroyl glutamate on the structure of proteins monitored by agarose native gel electrophoresis and circular dichroism

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
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Abstract

We have studied binding properties of three detergents, i.e., sodium dodecyl sulfate (SDS), Sarkosyl and sodium lauroyl glutamate (SLG), to model proteins based on their effects on electrophoretic mobilities of the proteins using agarose native gel electrophoresis and circular dichroism (CD). This simple technology can evaluate the dissociative properties of bound detergents from the proteins and their effects on protein structure. SDS influenced the electrophoretic mobilities of all model proteins more strongly than the other two detergents, implying a stronger inclination for protein binding and subsequent alterations in protein structure or reductions in activity, which are supported by CD analysis. On the contrary, Sarkosyl and SLG showed weaker binding and interfered less with the structure and biological activities, indicating that these detergents may be useful for protein purification and analysis. It appeared that SLG was weaker in protein binding than Sarkosyl, although the effects of these two detergents appeared to depend on the proteins.

Abstract Image

十二烷基硫酸钠、Sarkosyl 和月桂酰谷氨酸钠对琼脂糖原生凝胶电泳和圆二色性监测蛋白质结构的影响
我们利用琼脂糖原生凝胶电泳和圆二色性(CD)技术,研究了十二烷基硫酸钠(SDS)、Sarkosyl 和月桂酰谷氨酸钠(SLG)这三种去垢剂与模型蛋白质的结合特性及其对蛋白质电泳迁移率的影响。这种简单的技术可以评估与蛋白质结合的洗涤剂的解离特性及其对蛋白质结构的影响。与其他两种去垢剂相比,SDS 对所有模型蛋白质的电泳迁移率的影响更大,这意味着蛋白质结合的倾向性更强,随后会改变蛋白质的结构或降低其活性,CD 分析也证实了这一点。相反,Sarkosyl 和 SLG 的结合力较弱,对蛋白质结构和生物活性的干扰较小,表明这些去垢剂可用于蛋白质的纯化和分析。尽管这两种去垢剂的作用似乎取决于蛋白质,但 SLG 的蛋白质结合力似乎比 Sarkosyl 弱。
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来源期刊
Biophysical chemistry
Biophysical chemistry 生物-生化与分子生物学
CiteScore
6.10
自引率
10.50%
发文量
121
审稿时长
20 days
期刊介绍: Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.
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