The formation of amyloid fibrils is a self-assembly process of peptides or proteins. The superior mechanical properties of these fibrils make them interesting for materials science, but constitute a problem in amyloid-related diseases. Amyloid structures tend to be polymorphic and their structure depends on growth conditions. To understand and control the assembly process, insights into the relation between the mechanical properties and molecular structure are essential. We prepared long, straight as well as short, worm-like β-lactoglobulin amyloid fibrils and determined their morphology and persistence length by atomic force microscopy (AFM) and the molecular conformation using vibrational sum-frequency generation (VSFG) spectroscopy. We show that long fibrils with near-100% β-sheet content have a 40-times higher persistence length than short, worm-like fibrils with β-sheet contents below 80%.

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Persistent URL dx.doi.org/10.1021/ja206513r
Journal J. Am. Chem. Soc.
Citation
vandenAkker, C.C, Engel, M.F.M, Velikov, K.P, Bonn, M, & Koenderink, G.H. (2011). Morphology and bending rigidity of amyloid fibrils are correlated to peptide molecular structure. J. Am. Chem. Soc., 133(45), 18030–18033. doi:10.1021/ja206513r