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AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon

机译：基于原子力显微镜的力胰高血糖素成熟淀粉样蛋白原纤维的光谱测定

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摘要

We report on the mechanical characterization of individual mature amyloid fibrils by atomic force microscopy (AFM) and AFM-based single-molecule force spectroscopy (SMFS). These self-assembling materials, formed from the 29-residue amphiphatic peptide hormone glucagon, were found to display a reversible elastic behaviour. Based on AFM morphology and SMFS studies, we suggest that the observed elasticity is due to a force-induced conformational transition which is reversible due to the beta-helical conformation of protofibrils, allowing a high degree of extension. The elastic properties of such mature fibrils contribute to their high stability, suggesting that the internal hydrophobic interactions of amyloid fibrils are likely to be of fundamental importance in the assembly of amyloid fibrils and therefore for the understanding of the progression of their associated pathogenic disorders. In addition, such biological amyloid fibril structures with highly stable mechanical properties can potentially be used to produce nanofibres (nanowires) that may be suitable for nanotechnological applications.
机译：我们通过原子力显微镜（AFM）和基于AFM的单分子力谱（SMFS）报告单个成熟的淀粉样蛋白原纤维的机械特性。这些由29个残基的两亲肽激素胰高血糖素形成的自组装材料显示出可逆的弹性行为。基于AFM形态学和SMFS研究，我们建议观察到的弹性是由于力引起的构象转变，由于原纤的β螺旋构象是可逆的，从而允许高度延伸。这种成熟原纤维的弹性性质有助于它们的高稳定性，这表明淀粉样纤维的内部疏水相互作用在淀粉样纤维的组装中可能是最重要的，因此对于理解其相关的病原性疾病的进展也很重要。另外，具有高度稳定的机械性能的此类生物淀粉样蛋白原纤维结构可潜在地用于生产可能适用于纳米技术应用的纳米纤维（纳米线）。

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