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Effect of Helical Flanking Sequences on the Morphology of Polyglutamine-Containing Fibrils

机译：螺旋侧翼序列对聚谷氨酰胺原纤维形态的影响

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A peptide model system has been developed to study the effects of helical flanking sequences on polyglutamine aggregation. In a companion manuscript, the kinetics of aggregation are described, comparing the influence of a welldefined heterotetrameric coiled coil to that of the helix-rich structure found in Htt~(NT), a 17-residue flanking sequence found in the huntingtin protein, on polyglutamine aggregation. Here, the morphological characterization of the resultant fibrils that form for a set of peptides is reported, only one of which, KKQ_(25)KK, has been previously studied. A careful analysis of TEM and AFM images of KKQ_(25)KK confirms that it forms bundled fibrils of varying length and reveals, unexpectedly, that they are composed of fully extended cross-β-strands. Second, it is shown that helical flanking sequences do not disrupt the assembly of a core cross-β-sheet structure, but such flanking sequences can influence higher order processes, such as inhibiting the bundling of the fibrils.
机译：已经开发了一种肽模型系统来研究螺旋侧翼序列对聚谷氨酰胺聚集的影响。在同伴手稿中，描述了聚集的动力学，将定义明确的异四聚体卷曲螺旋与在亨廷顿蛋白中发现的17个残基侧翼序列Htt〜（NT）中发现的富含螺旋结构的影响进行了比较。聚谷氨酰胺聚集。在此，报道了形成为一组肽的所得原纤维的形态学表征，先前仅研究了其中之一KKQ_（25）KK。仔细分析KKQ_（25）KK的TEM和AFM图像，确认它形成了不同长度的成束原纤维，并出乎意料地揭示了它们由完全延伸的交叉β-链组成。第二，表明螺旋侧翼序列不会破坏核心交叉β-折叠结构的组装，但是这种侧翼序列会影响更高阶的过程，例如抑制原纤维的束缚。

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