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首页> 外文期刊>Biochemistry >A beta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution
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A beta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution

机译：淀粉样肽的β（1-28）片段在酸性溶液中主要采用多脯氨酸II构象

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摘要

To structurally characterize the nonaggregated state of the amyloid p peptide, which assembles into the hallmark fibrils of Alzheimer disease, we investigated the conformation of the N-terminal extracellular peptide fragment Abeta(t-28) in D2O at acidic pD by utilizing combined FTIR and isotropic and anisotropic Raman spectra measured between 1550 and 1750 cm(-1). Peptide aggregation is avoided under the conditions chosen. The amide I' band was found to exhibit a significant noncoincidence effect in that the first moment of the anisotropic Raman and of the IR band profile appears red-shifted from that of the isotropic Raman scattering. A simulation based on a coupled oscillator model involving all 27 amide I' modes of the peptide reveals that the peptide adopts a predominantly polyproline II conformation. Our results are inconsistent with the notion that the monomeric form of Abeta(1-28) is a totally disordered, random-coil structure. Generally, they underscore the notion that polyproline II is a characteristic motif of the unfolded state of proteins and peptides.
机译：为了在结构上表征淀粉样蛋白p肽的非聚集状态，该状态聚集到阿尔茨海默病的标志性原纤维中，我们通过结合使用FTIR和在1550至1750 cm（-1）之间测得的各向同性和各向异性拉曼光谱。在选择的条件下避免肽聚集。发现酰胺I'带表现出显着的非巧合效果，因为各向异性拉曼和IR带分布的第一矩​​出现了与各向同性拉曼散射的红移。基于涉及该肽的所有27种酰胺I'模式的耦合振荡器模型的仿真显示，该肽主要采用多脯氨酸II构象。我们的结果与Abeta（1-28）的单体形式是完全无序的随机线圈结构的概念不一致。通常，他们强调了聚脯氨酸II是蛋白质和肽的未折叠状态的特征性基序的观点。

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