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本文引用的文献

1
A kinetic model for beta-amyloid adsorption at the air/solution interface and its implication to the beta-amyloid aggregation process.β-淀粉样蛋白在气/液界面吸附的动力学模型及其对β-淀粉样蛋白聚集过程的影响。
J Phys Chem B. 2009 Mar 12;113(10):3160-8. doi: 10.1021/jp8085792.
2
Membrane-bound alpha-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles.膜结合的α-突触核蛋白形成一个延伸的螺旋结构：使用囊泡、双分子层和棒状胶束进行的长距离脉冲电子自旋共振测量。
J Am Chem Soc. 2008 Oct 1;130(39):12856-7. doi: 10.1021/ja804517m. Epub 2008 Sep 6.
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Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein.囊泡结合型α-突触核蛋白螺旋的反平行排列
J Am Chem Soc. 2008 Jun 25;130(25):7796-7. doi: 10.1021/ja801594s. Epub 2008 May 31.
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Infrared reflection-absorption spectroscopy and polarization-modulated infrared reflection-absorption spectroscopy studies of the organophosphorus acid anhydrolase langmuir monolayer.有机磷酸酐酶朗缪尔单分子层的红外反射吸收光谱和偏振调制红外反射吸收光谱研究。
J Phys Chem B. 2008 Apr 24;112(16):5250-6. doi: 10.1021/jp709591e. Epub 2008 Mar 29.
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Infrared reflection-absorption spectroscopy and polarization-modulated infrared reflection-absorption spectroscopy studies of the aequorin langmuir monolayer.水母发光蛋白朗缪尔单分子层的红外反射吸收光谱和偏振调制红外反射吸收光谱研究
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Changes in interfacial properties of alpha-synuclein preceding its aggregation.
Analyst. 2008 Jan;133(1):76-84. doi: 10.1039/b712812f. Epub 2007 Oct 15.
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Determination of alpha-synuclein concentration in human plasma using ELISA.使用酶联免疫吸附测定法测定人血浆中α-突触核蛋白的浓度。
Scand J Clin Lab Invest. 2007;67(4):431-5. doi: 10.1080/00365510601161497.
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The aggregation and fibrillation of alpha-synuclein.α-突触核蛋白的聚集和纤维化
Acc Chem Res. 2006 Sep;39(9):628-34. doi: 10.1021/ar050073t.
9
Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements.通过脉冲电子自旋共振测量得到的溶血磷脂酰胆碱胶束结合α-突触核蛋白中的螺旋间距离。
J Am Chem Soc. 2006 Aug 9;128(31):10004-5. doi: 10.1021/ja063122l.
10
Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers.α-突触核蛋白的结构、翻译后修饰及可变剪接作为聚集增强因子
Acta Neuropathol. 2006 Sep;112(3):237-51. doi: 10.1007/s00401-006-0104-6. Epub 2006 Jul 15.

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.

DOI:10.1039/c0cc02098b
PMID:20714568
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3186058/
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。