Abstract
Monosialoganglioside GM1-bound amyloid β-peptides have been found in patients' brains exhibiting early pathological changes of Alzheimer's disease. Herein, we report the ability of non-micellar GM1 to modulate Aβ(40) aggregation resulting in the formation of stable, short, rod-like, and cytotoxic Aβ(40) protofibrils with the ability to potentiate both Aβ(40) and Aβ(42) aggregation.