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Article

Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth.

Journal of the American Chemical Society - 23 Mar 2011

Qiang Wei, Yau Wai-Ming, Tycko Robert

Abstract excerpt

Structural variations in β-amyloid fibrils are potentially important to the toxicity of these fibrils in Alzheimer's disease (AD). We describe a repeated seeding protocol that selects a homogeneous fibril structure from a polymorphic initial state in the case of 40-residue β-amyloid fibrils with the Asp23-to-Asn, or Iowa, mutation (D23N-Aβ(1-40)). We use thioflavin T (ThT) fluorescence, transmission electron...

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Identifiers

PMID: 21355554
DOI: 10.1021/ja109679q
PMCID: PMC3060308

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

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