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Amyloid structure and assembly : insights from scanning transmission electron microscopy
Journal
Journal of structural biology
Volume
173
Number
1
Pages / Article-Number
1-13
Keywords
Amyloid, Mass measurement, Fibril, Filament, Oligomer, Protein aggregation, Electron microscopy, Scanning transmission electron microscopy, STEM, Alzheimer Disease, Type 2 Diabetes Mellitus, Prion, Scrapie, Yeast, Fungi
Abstract
Amyloid fibrils are filamentous protein aggregates implicated in several common diseases such as Alzheimer's disease and type II diabetes. Similar structures are also the mol. principle of the infectious spongiform encephalopathies such as Creutzfeldt-Jakob disease in humans, scrapie in sheep, and of the so-called yeast prions, inherited non-chromosomal elements found in yeast and fungi. Scanning transmission electron microscopy (STEM) is often used to delineate the assembly mechanism and structural properties of amyloid aggregates. In this review we consider specifically contributions and limitations of STEM for the investigation of amyloid assembly pathways, fibril polymorphisms and structural models of amyloid fibrils. This type of microscopy provides the only method to directly measure the mass-per-length (MPL) of individual filaments. Made on both in vitro assembled and ex vivo samples, STEM mass measurements have illuminated the hierarchical relationships between amyloid fibrils and revealed that polymorphic fibrils and various globular oligomers can assemble simultaneously from a single polypeptide. The MPLs also impose strong constraints on possible packing schemes, assisting in mol. model building when combined with high-resoln. methods like solid-state NMR (NMR) and ESR (EPR). [on SciFinder (R)]
