Conformation of Pyroglutamated Amyloid β (3-40) and (11-40) Fibrils - Extended or Hairpin?

ABSTRACT: Amyloid β (Aβ) is a hallmark protein of Alzheimer's disease. One physiologically important Aβ variant is formed by initial N-terminal truncation at a glutamic acid position (either E₃ or E₁₁), which is subsequently cyclized to a pyroglutamate (either pE₃ or pE₁₁). Both forms have been found in high concentrations in the core of amyloid plaques and are likely of high importance in the pathology of Alzheimer's disease. However, the molecular structure of the fibrils of these variants is not entirely clear. Solid-state NMR spectroscopy studies have reported a molecular contact between Gly₂₅ and Ile₃₁, which would disagree with the conventional hairpin model of wildtype (WT-)Aβ_1-40 fibrils, most often described in the

SUBMITTER: Scheidt HA 

PROVIDER: S-EPMC10895672 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature