Amyloid formation is associated with various neurodegenerative diseases. Therefore, extensive studies have been devoted to elucidating the structure, thermodynamic stability and assembly mechanisms of amyloid fibrils. In comparison, however, few studies have focused on the dynamics of amyloid fibrils, perhaps due to the fact that such fibrils are composed of highly-ordered and tightly-packed beta-sheets. Despite this crystal-like behavior, we find, using a model amyloid beta peptide and time-resolved infrared spectroscopy, that amyloid fibrils can still exhibit ultrafast conformational and hydrogen-bonding dynamics. We postulate that such ultrafast motions contribute to the total entropy of the system, hence playing an important role in stabilizing the underlying fibril structure.<br/>

Ultrafast dynamics in amyloid fibrils

256th National Meeting (2018)

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