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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >The effect of fulvic acid on pre- and postaggregation state of A??17-42: Molecular dynamics simulation studies
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The effect of fulvic acid on pre- and postaggregation state of A??17-42: Molecular dynamics simulation studies

机译：黄腐酸对A ?? 17-42聚集前后状态的影响：分子动力学模拟研究

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Alzheimer's disease (AD), a neurodegenerative disorder, is directly related to the aggregation of A?? peptides. These peptides can self-assemble from monomers to higher oligomeric or fibrillar structures in a highly ordered and efficient manner. This self-assembly process is accompanied by a structural transition of the aggregated proteins from their normal fold into a predominantly ??-sheet secondary structure. 14 ns molecular dynamics simulation revealed that fulvic acid interrupted the dimer formation of A??17-42 peptide while in its absence A??17-42 dimer formation occurred at ?? 12 ns. Additionally, fulvic acid disrupted the preformed A??17-42 trimer in a very short time interval (12 ns). These results may provide an insight in the drug design against A??17-42 peptide aggregation using fulvic acid as lead molecule against A??17-42 mediated cytotoxicity and neurodegeneration. ? 2012 Elsevier B.V. All rights reserved.
机译：神经退行性疾病阿尔茨海默氏病（AD）与Aβ的聚集直接相关肽。这些肽可以以高度有序和有效的方式从单体自组装成更高的寡聚或原纤维结构。这种自组装过程伴随着聚集蛋白从其正常折叠到主要为β-折叠二级结构的结构转变。 14 ns的分子动力学模拟表明，富叶酸中断了Aβ17-42肽的二聚体形成，而在缺少它的情况下，Aβ17-42的二聚体形成发生在Δβ17。 12 ns。另外，黄腐酸在很短的时间间隔（12ns）内破坏了预制的Aβ17-42三聚体。这些结果可以为使用Av 17-42介导的细胞毒作用和神经退行性变的富里酸作为先导分子对A 17 17-42肽聚集的药物设计提供一个见识。 ？ 2012 Elsevier B.V.保留所有权利。

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