α-突触核蛋白在气-液界面的α-螺旋构象：在其积累/聚集过程中构象和取向变化的意义。
Alpha-synuclein in alpha-helical conformation at air-water interface: implication of conformation and orientation changes during its accumulation/aggregation.
机构信息
California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA 90032, USA.
出版信息
Chem Commun (Camb). 2010 Sep 28;46(36):6702-4. doi: 10.1039/c0cc02098b. Epub 2010 Aug 16.
Abstract
Alpha-synuclein, a natively unstructured protein important in the neuropathology of Parkinson's disease, was found to form a Langmuir monolayer in an alpha-helical conformation with its helical axis parallel to the air-water interface. This study sheds light on the role of vesicles in neuronal cells in the accumulation/aggregation of alpha-synuclein.
摘要
α-突触核蛋白是帕金森病神经病理学中的一种重要的天然无规卷曲蛋白，研究发现其在α-螺旋构象中形成朗缪尔单层，其螺旋轴与气-液界面平行。这项研究阐明了囊泡在神经元细胞中对于α-突触核蛋白的积累/聚集的作用。
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