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Interaction of Hsp90 with phospholipid model membranes

文献类型： 外文期刊

作者： Zhang, Muhan 1 ; Wang, Daoying 1 ; Li, Pengpeng 1 ; Sun, Chong 1 ; Xu, Rong 1 ; Geng, Zhiming 1 ; Xu, Weimin 1 ; Dai, Zha 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Jiangsu, Peoples R China

2.Jiangsu Collaborat Innovat Ctr Meat Prod & Proc, Qual & Safety Control, Nanjing 210095, Jiangsu, Peoples R China

关键词： Hsp90;Lipid binding;Membrane;SPR

期刊名称：BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES （ 影响因子：3.747； 五年影响因子：4.404 ）

ISSN： 0005-2736

年卷期： 2018 年 1860 卷 2 期

页码：

收录情况： SCI

摘要： Heat shock protein 90 (Hsp90) is an essential molecular chaperone with versatile functions in cell homeostatic control under both normal and stress conditions. Hsp90 has been found to be expressed on the cell surface, but the mechanism of Hsp90 association to the membrane remains obscure. In this study, the direct interaction of Hsp90 and phospholipid vesicles was characterized, and the role of Hsp90 on membrane physical state was explored. Using surface plasmon resonance (SPR), we observed a strong interaction between Hsp90 and different compositions of lipid. Hsp90 had a preference to bind with more unsaturated phospholipid species and the affinity was higher with negatively charged lipids than zwitterionic lipids. Increasing the mole fraction of cholesterol in the phospholipid led to a decrease of binding affinity to Hsp90. Circular dichroism (CD) spectroscopy of Hsp90 in PC membranes showed more alpha-helix structure than in aqueous buffer. The differential scanning calorimeter (DSC) and fluorescence polarization results showed Hsp90 could affect the transition temperature and fluidity of the bilayer. We postulate from these results that the association between Hsp90 and membranes may involve both electrostatic and hydrophobic force, and constitute a possible mechanism that modulates membrane lipid order during thermal fluctuations.

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