期刊
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
卷 495, 期 -, 页码 30-38出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfa.2016.01.051
关键词
Gemini quaternary ammonium surfactants; Single-chain quaternary ammonium surfactants; Human serum albumin (HSA); Fluorescence spectroscopy; Dynamic lights scattering; Zeta potential
资金
- National Natural Science Foundation of China [21073164, 21473157]
The interactions of human serum albumin (HSA) with four cationic gemini surfactants and four single chain surfactants have been investigated from the measurements of fluorescence spectroscopy, dynamic lights scattering (DLS), zeta potential, and circular dichroism (CD). The fluorescence results show the binding strength of surfactants to HSA, along with the blue shift under the maximum emission wavelength (lambda(max)) which is sensitive to the protein conformations. It has been found that the hydrodynamic diameters of the protein aggregates are enlarged and the electrokinetic potentials of them get positive with increasing the concentration of the surfactants. The conformational transformation of the secondary structures of surfactant-HSA aggregates has been confirmed through the quantitative analysis of the CD spectra. The isothermal titration microcalorimetry (ITC) has been employed to further analyze the binding process of single-chain surfactants to HSA. The comprehensive results obtained from various approaches have shown that both hydrophobic and electrostatic interactions are present in the cationic surfactant-HSA systems. Compared with the corresponding single-chain surfactants, the gemini ones have much stronger binding ability to induce the unfolding of HSA. These investigations on the interactions between HSA and surfactants with the altered chain architecture in different concentration regimes can facilitate the application of surfactant-protein systems in pharmaceutical, biotechnology and related fields. (C) 2016 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据