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首页> 外文期刊>Journal of Non-Crystalline Solids: A Journal Devoted to Oxide, Halide, Chalcogenide and Metallic Glasses, Amorphous Semiconductors, Non-Crystalline Films, Glass-Ceramics and Glassy Composites >Amyloid-like self-assembly of a dodecapeptide sequence from the adenovirus fiber shaft: Perspectives from molecular dynamics simulations
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Amyloid-like self-assembly of a dodecapeptide sequence from the adenovirus fiber shaft: Perspectives from molecular dynamics simulations

机译：腺病毒纤维轴上十二肽序列的淀粉样样自组装：分子动力学模拟的观点

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摘要

Peptide and protein self-assembly is related to the fundamental problems of protein folding and misfolding and has potential applications in medicine, materials science and nanotechnology. Sequence repeats from self-assembling proteins may provide useful elementary building blocks of peptide-based nanostructures. Sequences from the adenovirus fiber shaft self-assemble into amyloid-like fibrils outside their native context. In earlier simulations we studied the self-assembly of two shaft sequences, the octapeptide NSGAITIG and the hexapeptide GAITIG. Based on these simulations, cysteine residues were substituted at the first two positions of the octapeptide, yielding amyloid fibrils capable of binding to silver, gold and platinum nanoparticles. Here, we study by implicit-solvent replica-exchange simulations the self-assembly of a longer shaft sequence, the dodecapeptide LSFDNSGAITIG. The simulations provide insights on the molecular organization of the corresponding fibers. Individual molecules tend to adopt hairpin-like conformations in the observed intermolecular β-sheets, in line with the experimentally determined amyloid fiber diameters and the conformation of the peptide in the adenovirus fiber shaft. By analyzing the arrangement of individual peptides in the intermolecular sheets, we suggest possible structural models of the corresponding fibers and interpret their stability by energetic calculations.
机译：肽和蛋白质的自组装与蛋白质折叠和错误折叠的基本问题有关，在医学，材料科学和纳米技术中具有潜在的应用。自组装蛋白的序列重复可以提供有用的基于肽的纳米结构的基本结构单元。腺病毒纤维轴的序列在其天然环境外自组装成淀粉样蛋白原纤维。在较早的模拟中，我们研究了八肽NSGAITIG和六肽GAITIG两个轴序列的自组装。基于这些模拟，半胱氨酸残基在八肽的前两个位置被取代，产生能够与银，金和铂纳米粒子结合的淀粉样原纤维。在这里，我们通过隐式溶剂复制-交换模拟研究更长轴序列的自组装，即十二肽LSFDNSGAITIG。模拟提供了有关相应纤维的分子组织的见解。与实验确定的淀粉样蛋白纤维直径和腺病毒纤维轴中肽的构象一致，单个分子倾向于在观察到的分子间β-折叠中采用发夹样构象。通过分析分子间薄片中单个肽的排列，我们建议了相应纤维的可能结构模型，并通过能量计算来解释其稳定性。

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