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首页> 外文期刊>RSC Advances >Triphala inhibits alpha-synuclein fibrillization and their interaction study by NMR provides insights into the self-association of the protein
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Triphala inhibits alpha-synuclein fibrillization and their interaction study by NMR provides insights into the self-association of the protein

机译：Triphala抑制α-突触核蛋白的原纤化及其NMR的相互作用研究为蛋白质的自我关联提供了见解

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摘要

The process of assembly and accumulation of the intrinsically disordered protein (IDP), alpha-synuclein (αSyn) into amyloid fibrils is a pathogenic process leading to several neurodegenerative disorders such as Parkinson's disease, multiple system atrophy and others. Although several molecules are known to inhibit αSyn fibrillization, the mechanism of inhibition is just beginning to emerge. Here, we report the inhibition of fibrillization of αSyn by Triphala, a herbal preparation in the traditional Indian medical system of Ayurveda. Triphala was found to be a rich source of polyphenols which are known to act as amyloid inhibitors. ThT fluorescence and TEM studies showed that Triphala inhibited the fibrillization of αSyn. However, it was observed that Triphala does not disaggregate preformed αSyn fibrils. Further, native-PAGE showed that Triphala reduces the propensity of αSyn to oligomerize during the lag phase of fibrillization. Our NMR results showed that certain stretches of residues in the N-terminal and NAC regions of αSyn play an anchor role in the self-association process of the protein, thereby providing mechanistic insights into the early events during αSyn fibrillization.
机译：本质上无序蛋白质（IDP），α-突触核蛋白（αsyn）的组装和积累成淀粉样蛋白原纤维是一种致病方法，导致几种神经变性疾病，如帕金森病，多种系统萎缩等。虽然已知几种分子抑制αsyn纤维化，但抑制机制恰好开始出现。在这里，我们报告了Triphala抑制αsyn的原纤化，在Ayurveda的传统印度医疗系统中的草药制剂。发现Triphala是一种丰富的多酚来源，已知用作淀粉样蛋白抑制剂。 THT荧光和TEM研究表明，三麦植物抑制了αsyn的原纤化。然而，观察到Triphala不会分解预成形的αsyn原纤维。此外，本地页面表明，三卤代在原纤化的滞后阶段期间降低了αsyn的倾向。我们的NMR结果表明，αSyn的N-末端和NAC区域中的某些残留物在蛋白质的自我关联过程中发挥着锚作用，从而在αSyn纤维化期间提供了在早期事件中的机械洞察力。

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