纤维
淀粉样纤维
表征(材料科学)
纳米尺度
力谱学
原子力显微镜
刚度
淀粉样蛋白(真菌学)
破损
材料科学
动力学
生物物理学
结晶学
化学
纳米技术
淀粉样β
复合材料
生物化学
生物
病理
无机化学
物理
医学
疾病
量子力学
作者
J. F. Smith,Tuomas P. J. Knowles,Christopher M. Dobson,Cait E. MacPhee,Mark E. Welland
标识
DOI:10.1073/pnas.0604035103
摘要
We report the detailed mechanical characterization of individual amyloid fibrils by atomic force microscopy and spectroscopy. These self-assembling materials, formed here from the protein insulin, were shown to have a strength of 0.6 +/- 0.4 GPa, comparable to that of steel (0.6-1.8 GPa), and a mechanical stiffness, as measured by Young's modulus, of 3.3 +/- 0.4 GPa, comparable to that of silk (1-10 GPa). The values of these parameters reveal that the fibrils possess properties that make these structures highly attractive for future technological applications. In addition, analysis of the solution-state growth kinetics indicated a breakage rate constant of 1.7 +/- 1.3 x 10(-8) s(-1), which reveals that a fibril 10 mum in length breaks spontaneously on average every 47 min, suggesting that internal fracturing is likely to be of fundamental importance in the proliferation of amyloid fibrils and therefore for understanding the progression of their associated pathogenic disorders.
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