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作 者:李爱学[1,2] 崔小强[1] 杨帆[1] 杨秀荣[1]
机构地区:[1]中国科学院长春应用化学研究所电分析化学国家重点实验室,长春130022 [2]中国科学院研究生院,北京100039
出 处:《分析化学》2009年第1期25-29,共5页Chinese Journal of Analytical Chemistry
基 金:国家自然科学基金(No.90713022);国家重点基础研究规划项目(No.2007CB714500);中国科学院创新基金(No.kJCX2-YW-H11,kJCX2-YW-H09)资助项目
摘 要:细胞膜的内膜含有大量的负电荷磷脂,研究F-肌动蛋白与负电荷磷脂的相互作用将有助于更深入地了解细胞骨架与细胞膜的体内相互作用机制。在金片和金电极上分别构建了负电荷磷脂的杂化双层磷脂膜,通过表面等离子体共振方法(SPR)和电化学阻抗技术研究了F-肌动蛋白与负电荷磷脂膜的相互作用。结果表明,F-肌动蛋白可以在没有中间联系蛋白的情况下,直接与负电荷磷脂膜发生相互作用。钙离子可以有效地促进它们的相互作用,表明钙离子在其中发挥了重要作用。高浓度的KCl显著抑制它们的相互作用,表明这种相互作用主要受静电作用影响。实验结果进一步证明在F-肌动蛋白与负电荷磷脂膜相互作用时,除了可以通过其它蛋白发生间接相互作用外,还可以与磷脂膜发生直接的相互作用。Actin is a ubiquitous eytoskeletal protein involved in many fundamental cellular processes. In the cell, aetin generally performs its functions in its polymerized form (F-actin). It is well known that the interior membrane of the natural membranes contains a large amount of negatively charged lipids, so the study of the interaction between F-actin and negatively charged lipids would bring some insight on the interaction between the cytoskeleton and the cell membrane in vivo. The interaction of F-actin and negatively charged lipids membrane has been investigated by surface plasmon resonance and electrochemical impedance spectroscopy. The result shows that F-actin can interact with the negatively charged lipids membrane directly without any intermediate linker protein. Ca^2+ can effectively promote this interaction, indicating that in this case the divalent cations played an important role. High concentrations of KC1 will inhibit this interaction significantly, indica- ting that the interaction between F-actin and negatively charged lipid membrane is mainly dominated by elec- trostatic interactions, although other forces also involved. The results confirm that two mechanisms of the interaction between F-actin and the lipids membrane may exist: direct interaction with lipids and interaction through other membrane protein.
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