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首页> 外文期刊>Biochemistry >Role of Protein-Water Interactions and Electrostatics in alpha-Synuclein Fibril Formation.
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Role of Protein-Water Interactions and Electrostatics in alpha-Synuclein Fibril Formation.

机译：蛋白质-水相互作用和静电在α-突触核蛋白原纤维形成中的作用。

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摘要

Deposition of misfolded alpha-synuclein is a critical factor in several neurodegenerative disorders. Filamentous alpha-synuclein is the major component of Lewy bodies and Lewy neurites, the intracellular inclusions in the dopaminergic neurons of the substantia nigra, which are considered the pathological hallmark of Parkinson's disease. We show here that anions induce partial folding of alpha-synuclein at neutral pH, forming a critical amyloidogenic intermediate, which leads to significant acceleration of the rate of fibrillation. The magnitude of the accelerating effect generally followed the position of the anions in the Hofmeister series, indicating a major role of protein-water-anion interactions in the process at salt concentrations above 10 mM. Below this concentration, electrostatic effects dominated in the mechanism of anion-induced fibrillation. The acceleration of fibrillation by anions was also dependent on the cation. Moderate concentrations of anions affected both the rates of nucleation and the elongation of alpha-synuclein fibrillation, primarily via their effect on the interaction of the protein with water.
机译：错误折叠的α-突触核蛋白的沉积是几种神经退行性疾病的关键因素。丝状α-突触核蛋白是路易体和路易神经突的主要成分，是黑质的多巴胺能神经元的细胞内包裹体，被认为是帕金森氏病的病理标志。我们在这里显示阴离子在中性pH值下诱导α-突触核蛋白的部分折叠，形成关键的淀粉样生成中间体，从而导致原纤化速率显着加速。加速作用的大小通常跟随阴离子在Hofmeister系列中的位置，这表明在盐浓度高于10 mM的过程中蛋白质-水-阴离子相互作用的主要作用。低于此浓度，静电作用在阴离子诱导的原纤化机理中起主导作用。阴离子对原纤维的加速作用还取决于阳离子。中等浓度的阴离子主要通过它们对蛋白质与水相互作用的影响，影响成核速率和α-突触核蛋白原纤化的伸长。

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