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Destabilization of amyloid fibrils on interaction with MoS2-based nanomaterials

机译：淀粉样蛋白原纤维的稳定化与MOS2基纳米材料相互作用

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The present work is motivated by the established concept that the structure and energetics of biomacromolecules can be modulated by confining their dimensions in the nanoscale. In particular, here we use force-field methods to understand the stability of amyloid fibrils at nanostructured interfaces, which can be useful for the development of new therapeutics for Alzheimer's disease. We explore the binding modes and structural properties of fibrils at the interface of molybdenum disulphide nanotubes and the nanosurface using classical molecular dynamics simulations. We find that in general the MoS _(2) materials induces disruptions in the structure of the amyloid fibrils where the beta sheet conformation of the fibrils changes to a turned conformation, and it is large in the case of nanotubes in comparison to the nanosurfaces. The intermolecular hydrogen bonds, hydrophilic and hydrophobic contacts between the monomer peptides in the fibril are reduced due to their adsorption onto the MoS _(2) materials, which results in a destabilization of the fibril. The destabilization of fibril is to some extent compensated for by the van der Waals interactions between the fibril and MoS _(2) . Overall the results indicate that MoS _(2) -based materials can be useful in inhibiting the aggregation of smaller protofibrils to matured fibrils and to bust the already formed fibrils. Therapeutic materials should not exhibit any cross interaction with other off-targets compounds. In order to test whether the MoS _(2) nanomaterial has any such effect we have studied its interaction with two additional biomacromolecules, the human serum albumin and p53 protein, and we report no significant changes in the secondary structure of these biomolecules. Through molecular docking studies we also established that the drug binding ability of HSA is not altered by its surface binding to MoS _(2) nanosurface.
机译：目前的作品是由既定的概念激励，即通过将纳米尺度限制它们的尺寸可以通过将其尺寸限制来调节生物致摩托的结构和能量。特别是，在这里，我们使用力现场方法来了解纳米结构界面处淀粉样蛋白原纤维的稳定性，这可用于开发阿尔茨海默病的新治疗方法。我们使用经典分子动力学模拟探索钼纳米管界面和纳米曲面界面处的原纤维的结合模式和结构性质。我们发现通常，MOS _（2）材料在淀粉样蛋白原纤维的结构中引起破坏，其中原纤维的β薄片构象变化为转向构象，并且在与纳米孔相比的纳米管的情况下很大。由于其吸附在MOS _（2）材料上，纤维中的单体氢键，在原纤维中的分子间氢键，亲水和疏水触点被降低，这导致原纤维的稳定性。原纤维的稳定化是通过丙烷和MOS _（2）之间的范德华相互作用来补偿的一定程度。总的来说，结果表明MOS _（2）基础的材料可用于抑制较小的原纤维的聚集，以达到成熟的原纤维并破坏已经形成的原纤维。治疗材料不应表现出与其他偏离靶向化合物的任何交叉相互作用。为了测试MOS _（2）纳米材料是否具有任何这种效果，我们研究了其与两种额外的生物致疣，人血清白蛋白和P53蛋白的相互作用，并且我们报告了这些生物分子的二级结构的显着变化。通过分子对接研究，我们还确定了HSA的药物结合能力不会通过其表面结合MOS _（2）纳米孔而改变。

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