title: Morphology and persistence length of amyloid fibrils are correlated to peptide molecular structure.
abstract: 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%.
authors: FOM Institute AMOLF, Science Park 104, 1098 XG, Amsterdam, The Netherlands.
authors: Corianne C
authors: CC
authors: vandenAkker
authors: Maarten F M
authors: MF
authors: Engel
authors: Krassimir P
authors: KP
authors: Velikov
authors: Mischa
authors: M
authors: Bonn
authors: Gijsje H
authors: GH
authors: Koenderink
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D010455:Peptides