Amyloid β-peptides 1-40 and 1-42 form oligomers with mixed β-sheets.

ABSTRACT: Two main amyloid-β peptides of different length (Aβ₄₀ and Aβ₄₂) are involved in Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and mixed oligomers may contribute to the toxic species. However, little is know about the extent of mixing. To study whether Aβ₄₀ and Aβ₄₂ co-aggregate, we used Fourier transform infrared spectroscopy in combination with ¹³C-labeling and spectrum calculation and focused on the amide I vibration, which is sensitive to backbone structure. Mixtures of monomeric labeled Aβ₄₀ and unlabeled Aβ₄₂ (and vice versa) were co-incubated for ∼20 min and their infrared spectrum recorded. The position of the main ¹³C-amide I' band shifted to hi

SUBMITTER: Baldassarre M 

PROVIDER: S-EPMC5857929 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature