Amyloidogenic aggregation of β-amyloid (Aβ) peptides disrupts cellular membranes and is a viable cytotoxicity mechanism in Alzheimer’s disease, but studying the underlying molecular behavior is challenging due to peptide heterogeneity and low abundance. Here, the authors use solid-state nuclear magnetic resonance spectroscopy to show that, compared to the less pathogenic Aβ1-40 peptide, Aβ1-42 forms smaller oligomers prior to fibrillation and exhibits more pronounced residue-specific contacts with phospholipid headgroups.
- Maurine K. Kengwerere
- June M. Kenyaga
- Wei Qiang
