Journal article

Sedimentation Velocity Analysis of the Size Distribution of Amyloid Oligomers and Fibrils

Yee-Foong Mok, Geoffrey J Howlett, Michael DW Griffin, JL Cole (ed.)

ANALYTICAL ULTRACENTRIFUGATION | ELSEVIER ACADEMIC PRESS INC | Published : 2015

Abstract

Amyloid fibrils result from the self-assembly of proteins into large aggregates with fibrillar morphology and common structural features. These fibrils form the major component of amyloid plaques that are associated with a number of common and debilitating diseases, including Alzheimer's disease. While a range of unrelated proteins and peptides are known to form amyloid fibrils, a common feature is the formation of aggregates of various sizes, including mature fibrils of differing length and/or structural morphology, small oligomeric precursors, and other less well-understood forms such as amorphous aggregates. These various species can possess distinct biochemical, biophysical, and patholog..

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