title: Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments.
abstract: Amyloid fibrils, originally associated with neurodegenerative diseases, are now recognized to have interesting mechanical properties. By using synchrotron x-ray diffraction at high pressure in a diamond anvil cell we determined the bulk modulus of TTR105-115 amyloid fibrils in water and in silicone oil to be 2.6 and 8.1 GPa, respectively. The compression characteristics of the fibrils are quite different in the two media, revealing the presence of cavities along the axis of the fibrils, but not between the β-sheets, which are separated by a dry interface as in a steric zipper motif. Our results emphasize the importance of peptide packing in determining the structural and mechanical properties of amyloid fibrils.
authors.affiliation: Department of Chemistry, Katholieke Universiteit Leuven, Leuven, Belgium, UK. filip.meersman@chem.kuleuven.be
authors.forename: Filip
authors.initials: F
authors.lastname: Meersman
authors.forename: Raúl Quesada
authors.initials: RQ
authors.lastname: Cabrera
authors.forename: Paul F
authors.initials: PF
authors.lastname: McMillan
authors.forename: Vladimir
authors.initials: V
authors.lastname: Dmitriev
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D055595:Mechanical Phenomena; D010455:Peptides / Q000737:chemistry*; D011228:Prealbumin / Q000737:chemistry*; D011312:Pressure; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D000682:Amyloid; D010455:Peptides; D011228:Prealbumin