Prevention of Amyloid-β Fibril Formation Using Antibodies Against the C-terminal Region of Amyloid-β1-40 and Amyloid-β1-42

Alzheimer's disease is characterized by the abnormal aggregation of amyloid-beta (A beta)(1-40) and A beta(1-42) peptides into fibrils. In this work, we analyzed the kinetics of A beta(1-40) and A beta(1-42) fibril formation in vitro using Thioflavin T fluorescence. We synthesized high-purity peptides and performed a hexafluoro-2-propanol pre-treatment to yield uniform peptide solutions as starting materials. We found that the aggregation is clearly affected by the presence of sub-millimolar quantities of antibodies against the C-terminal region of the peptides. Because the fibrillization of these peptides is closely related to the pathogenesis of Alzheimer's disease, blocking this process may provide significant therapeutic benefit.