Shear flow promotes amyloid-beta fibrilization
Dave E Dunstan, Paul Hamilton-Brown, Peter Asimakis, William Ducker, Joseph Bertolini
PROTEIN ENGINEERING DESIGN & SELECTION | OXFORD UNIV PRESS | Published : 2009
The rate of formation of amyloid fibrils in an aqueous solution of amyloid-beta (Abeta) is greatly increased when the solution is sheared. When Abeta solution is stirred with a magnetic stirrer bar at 37 degrees C, a rapid increase in thioflavin T fluorescence is observed. Atomic Force Microscopy (AFM) images show the formation of aggregates, the growth of fibrils and the intertwining of the fibrils with time. Circular dichroism (CD) spectroscopy of samples taken after stirring shows a transition from random coil to alpha-helix to beta-sheet secondary structure over 20 h at 37 degrees C. The fluorescence, AFM and CD measurements are all consistent with the formation of amyloid fibrils. Quies..View full abstract
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Awarded by Australian Research Council
The Australian Research Council Grant LP0562318 is acknowledged.