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Effects of Fluorinated and Hydrogenated Surfactants on Human Serum Albumin at Different pHs

机译:氟化和氢化表面活性剂对不同pH值下人血清白蛋白的影响

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摘要

Complexation between human serum albumin(HSA)and two different surfactants,one fully fluorinated(sodium perfluorooctanoate,SPFO)and one fully hydrogenated(sodium caprylate,SO),was studied using zeta-potential measurements and difference spectroscopy.The study was carried out at three different pHs,3.2,6.7,and 10.0.The spectroscopy study was performed at pHs 6.7 and 10.0,given that at pH 3.2 high turbidity was observed in the wide range of surfactant concentrations.The results were interpreted in terms of the electrostatic and hydrophobic contributions to the stability of the different phases formed in the water-surfactant-HSA system.Solutions and precipitates were observed in the concentration range investigated in more detail.Using Pace methods,the thermodynamic values of the surfactant-induced conformational changes in HSA were determined for sodium perfluorooctanoate in the concentration range 2-12 rnmol dm~(-3)at pH 6.7 and 5-22 mmol dm~(-3)at pH 10.0.Electrophoretic measurements were used to characterize surfactant adsorption by determining the number of molecules adsorbed on the surface of HSA and the Gibbs energy of adsorption.Finally,the interactions between human serum albumin and other anionic surfactants studied by other authors were compared with those observed in the present work.
机译:使用ζ电势测量和差光谱法研究了人血清白蛋白(HSA)与两种不同表面活性剂之间的络合,一种是完全氟化的(全氟辛酸钠,SPFO),另一种是完全氢化的(辛酸钠,SO)。三种不同的pH值3.2、6.7和10.0。在pH 6.7和10.0下进行了光谱研究,因为在pH 3.2的情况下,在各种浓度的表面活性剂中都观察到了高浊度。结果用静电和疏水性来解释在水-表面活性剂-HSA体系中形成的不同相的稳定性起着重要作用。在浓度范围内更详细地观察到溶液和沉淀物。使用Pace方法,确定了表面活性剂引起的HSA构象变化的热力学值在pH 6.7时浓度范围为2-12 rnmol dm〜(-3)和pH 10.0时浓度范围为5-22 mmol dm〜(-3)的全氟辛酸钠。通过测定HSA表面吸附的分子数量和吸附的吉布斯能来表征表面活性剂的吸附。最后,将其他作者研究的人血清白蛋白与其他阴离子表面活性剂之间的相互作用与本工作进行了比较。 。

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