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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy
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The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy

机译：amyloid-like肽原纤维结构的变化揭示了x射线散射、衍射和电子显微镜

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摘要

Structural analysis of protein fibrillation is inherently challenging. Given the crucial role of fibrils in amyloid diseases, method advancement is urgently needed. A hybrid modelling approach is presented enabling detailed analysis of a highly ordered and hierarchically organized fibril of the GNNQQNY peptide fragment of a yeast prion protein. Data from small-angle X-ray solution scattering, fibre diffraction and electron microscopy are combined with existing high-resolution X-ray crystallographic structures to investigate the fibrillation process and the hierarchical fibril structure of the peptide fragment. The elongation of these fibrils proceeds without the accumulation of any detectable amount of intermediate oligomeric species, as is otherwise reported for, for example, glucagon, insulin and beta-synuclein. Ribbons constituted of linearly arranged protofilaments are formed. An additional hierarchical layer is generated via the pairing of ribbons during fibril maturation. Based on the complementary data, a quasi-atomic resolution model of the protofilament peptide arrangement is suggested. The peptide structure appears in a beta-sheet arrangement reminiscent of the beta-zipper structures evident from high-resolution crystal structures, with specific differences in the relative peptide orientation. The complexity of protein fibrillation and structure emphasizes the need to use multiple complementary methods.
机译：结构分析的蛋白质纤维性颤动固有的挑战。纤维在淀粉样疾病,方法的进步是迫切需要的。启用详细的分析提出了高度有序的层级结构组织原纤维GNNQQNY肽片段的酵母朊病毒蛋白质。解决方案散射纤维衍射和结合现有的电子显微镜高分辨率x射线晶体结构探讨颤和过程层次肽的原纤维结构片段。没有任何的积累可检测的中间低聚物的物种,否则报告,例,胰高血糖素、胰岛素和beta-synuclein。丝带组成的线性排列的原丝形成。通过配对分级层生成丝带在原纤维的成熟。补充数据,quasi-atomic决议模型的原丝肽的安排建议。β褶板安排的从beta-zipper结构明显高分辨率的晶体结构,与特定的肽的相对差异取向。蛋白质纤维性颤动的复杂性强调需要使用多个结构互补的方法。

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