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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Dry amyloid fibril assembly in a yeast priori peptide is mediated by long-lived structures containing water wires
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Dry amyloid fibril assembly in a yeast priori peptide is mediated by long-lived structures containing water wires

机译：酵母先验肽中的干燥淀粉样蛋白原纤维装配是由包含水丝的长寿命结构介导的

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摘要

Amyloid-like fibrils from a number of small peptides that are unrelated by sequence adopt a cross-β-spine in which the two sheets fully interdigitate to create a dry interface. Formation of such a dry interface is usually associated with self-assembly of extended hydrophobic surfaces. Here we investigate how a dry interface is created in the process of protofilament formation in vastly different sequences using two amyloidogenic peptides, one a polar sequence from the N terminus of the yeast prion Sup35 and the other a predominantly hydrophobic sequence from the C terminus of Aβ-peptide. Using molecular dynamics simulations with three force fields we show that spontaneous formation of two ordered one-dimensional water wires in the pore between the two sheets of the Sup35 protofilaments results in long-lived structures, which are stabilized by a network of hydrogen bonds between the water molecules in the wires and the polar side chains in the (3-sheet. Upon decreasing the stability of the metastable structures, water molecules are expelled resulting in a helically twisted protofilament in which side chains from a pair of β-strands in each sheet pack perfectly resulting in a dry interface. Although drying in hydrophobically dominated interfaces is abrupt, resembling a liquid to vapor transition, we find that discrete transitions between the liquid to one-dimensional ordered water in the nanopore enclosed by the two (3-sheets to dry interface formation characterizes protofilament assembly in the yeast prions. Indeed, as the two sheets of the hydrophobic Aβ-sequence approach each other, fibril formation and expulsion of water molecules occur rapidly and nearly simultaneously.
机译：来自许多与序列无关的小肽的淀粉样样原纤维采用了交叉的β-脊柱，其中两个薄片完全相互交叉以形成干燥的界面。这种干燥界面的形成通常与延伸的疏水表面的自组装有关。在这里，我们研究了如何使用两种淀粉样蛋白生成肽在原丝形成过程中以不同的序列创建干燥界面，一种是来自酵母病毒Sup35 N端的极性序列，另一种是来自AβC端的疏水序列-肽。使用具有三个力场的分子动力学模拟，我们表明，在两张Sup35原型丝之间的孔中自发形成两条有序的一维水线会导致长寿命结构，并通过氢键之间的氢键网络使其稳定导线中的水分子和（3片中的）极性侧链。在降低亚稳结构的稳定性时，水分子被排出，导致螺旋扭曲的原丝，其中每片中一对β链的侧链虽然在疏水性支配的界面中突然干燥，类似于从液体到蒸气的转变，但我们发现，在液体和一维有序水之间的离散转变是由两个（3片干燥界面的形成是酵母病毒中原丝组装的特征，事实上，疏水性Aβ序列的两片彼此之间，原纤维的形成和水分子的排出迅速并几乎同时发生。

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