Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling

Marianna Török, Saskia Milton, Rakez Kayed, Peng Wu, Theresa McIntire, Charles G. Glabe, Ralf Langen

Research output: Contribution to journalArticle

321 Scopus citations

Abstract

Electron paramagnetic resonance spectroscopy analysis of 19 spin-labeled derivatives of the Alzheimer's amyloid β (Aβ) peptide was used to reveal structural features of amyloid fibril formation. In the fibril, extensive regions of the peptide show an in-register, parallel arrangement. Based on the parallel arrangement and side chain mobility analysis we find the amyloid structure to be mostly ordered and specific, but we also identify more dynamic regions (N and C termini) and likely turn or bend regions (around residues 23-26). Despite their different aggregation properties and roles in disease, the two peptides, Aβ40 and Aβ42, homogeneously co-mix in amyloid fibrils suggesting that they possess the same structural architecture.

Original languageEnglish (US)
Pages (from-to)40810-40815
Number of pages6
JournalJournal of Biological Chemistry
Volume277
Issue number43
DOIs
StatePublished - Oct 25 2002
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

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