膜联蛋白A1与两性离子磷脂单层的相互作用：荧光显微镜研究
Annexin A1 interaction with a zwitterionic phospholipid monolayer: a fluorescence microscopy study.
作者信息
Freites J Alfredo, Ali Shahla, Rosengarth Anja, Luecke Hartmut, Dennin Michael B
机构信息
Department of Physics and Astronomy and Institute for Surface and Interface Science, University of California, Irvine, California 92697-4575, USA.
出版信息
Langmuir. 2004 Dec 21;20(26):11674-83. doi: 10.1021/la049713b.
We present the results of a fluorescence microscopy study of the interaction of annexin A1 with dipalmitoylphosphatidylcholine (DPPC) monolayers as a function of the lipid monolayer phase and the pH of the aqueous subphase. We show that annexin A1-DPPC interaction depends strongly on the domain structure of the DPPC monolayer and only weakly on the subphase pH. Annexin A1 is found to be line active, with preferential adsorption at phase boundaries. Also, annexin A1 is found to form networks in the presence of a domain structure in the monolayer. Our results point toward an important contribution of the unique N-terminal domain to the organization of the protein at the interface.
我们展示了一项荧光显微镜研究的结果，该研究考察了膜联蛋白A1与二棕榈酰磷脂酰胆碱（DPPC）单层膜的相互作用，此相互作用是脂质单层膜相和水相亚相pH值的函数。我们表明，膜联蛋白A1与DPPC的相互作用强烈依赖于DPPC单层膜的畴结构，而对亚相pH值的依赖较弱。发现膜联蛋白A1具有线活性，在相界处优先吸附。此外，发现在单层膜存在畴结构的情况下，膜联蛋白A1会形成网络。我们的结果表明，独特的N端结构域对蛋白质在界面处的组织有重要贡献。
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