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Article

Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.

Journal of the American Chemical Society - 10 Aug 2016

Elkins Matthew R, Wang Tuo, Nick Mimi, Jo Hyunil, Lemmin Thomas, Prusiner Stanley B, DeGrado William F, Stöhr Jan, Hong Mei

Abstract excerpt

The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer and molecular scales. Various fibril growth conditions have been identified to cause polymorphism, but the intrinsic amino acid sequence basis for this polymorphism has been unclear. Several single-site mutations in the center of the Aβ sequence cause different disease phenotypes and fibrillization properties. The...

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Identifiers

PMID: 27414264
DOI: 10.1021/jacs.6b03715
PMCID: PMC5149419

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