Laboratory of Cellular Dynamics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
FEBS Lett. 2011 Nov 16;585(22):3513-9. doi: 10.1016/j.febslet.2011.10.006. Epub 2011 Oct 12.
Interactions of the presynaptic protein α-synuclein with membranes are involved in its physiological action as well as in the pathological misfolding and aggregation related to Parkinsons's disease. We studied the conformation and orientation of α-synuclein bound to model vesicular membranes using multiparametric response polarity-sensitive fluorescent probes together with CD and EPR measurements. At low lipid to α-synuclein ratio the protein binds membranes through its N-terminal domain. When lipids are in excess, the α-helical content and the role of the C-terminus in binding increase. Highly rigid membranes also induce a greater α-helical content and a lower polarity of the protein microenvironment.
突触前蛋白α-突触核蛋白与膜的相互作用与其生理作用有关，也与帕金森病相关的病理性错误折叠和聚集有关。我们使用多参数响应极性敏感荧光探针结合 CD 和 EPR 测量研究了与模型囊泡膜结合的α-突触核蛋白的构象和取向。在低脂质与α-突触核蛋白比例时，该蛋白通过其 N 端结构域结合膜。当脂质过量时，α-螺旋含量和 C 端在结合中的作用增加。高度刚性的膜也会诱导更高的α-螺旋含量和更低的蛋白质微环境极性。
