Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance.
A general method to explore the dynamic nature of amyloid fibrils is described, combining hydrogen/deuterium exchange and nuclear magnetic resonance spectroscopy to determine the exchange rates of individual amide protons within an amyloid fibril. Our method was applied to fibrils formed by the amyloid-beta(1-40) peptide, the major protein component of amyloid plaques in Alzheimer's disease. The fastest exchange rates were detected among the first 14 residues of the peptide, a stretch known to be poorly structured within the fibril. Considerably slower exchange rates were observed in the remainder of the peptide within the beta-strand-turn-beta-strand motif that constitutes the fibrillar core.
Olofsson
Anders
A
Umeå Center for Molecular Pathogenesis, Umeå University, Umeå, Sweden. anders.olofsson@ucmp.umu.se
Sauer-Eriksson
A Elisabeth
AE
Ohman
Anders
A
D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D041961:Deuterium Exchange Measurement / Q000379:methods*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation
D000682:Amyloid