Meinhardt J, Sachse C, Hortschansky P, Grigorieff N, Fändrich M.
Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils.
J Mol Biol. 2009 Feb 27;386(3):869-77.
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This is a very interesting and thorough analysis of the structural basis of Abeta1-40 fibril heterogeneity. Fibrils have remarkable heterogeneity even when grown under uniform conditions. Using cryoEM, the authors demonstrate that interprotofilament interactions are are quite variable, resulting in an ensemble of possible orientations within the fibril. One can only speculate about the significance of this heterogeneity on Alzheimer disease pathogenesis.