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Static and dynamic AFM studies of the effect of anti-Abeta antibodies on Abeta aggregates and their formation



Static and dynamic AFM studies of the effect of anti-Abeta antibodies on Abeta aggregates and their formation



Biophysical Journal 86(1): 152a



Extensive data suggest that the conversion of the amyloid-beta (Abeta) peptide from soluble to insoluble forms is a key factor in the pathogenesis of Alzheimer's disease (AD). In recent years, atomic force microscopy (AFM) has provided useful insights into the physicochemical processes involving Abeta, and it can now be used to investigate factors that either inhibit or promote fibrillogenesis. Recently, there has been considerable interest in the role of anti-Abeta monoclonal antibodies as potential inhibitors of Abeta fibrillogenesis, as disrupters of already formed aggregates, and as clinical diagnostic tools. This presentation will explore the use of AFM in understanding the impact of anti-Abeta antibodies directed against different domains of Abeta on various stages of fibril formation with particular focus on quantitative analysis of AFM images. Two antibodies were primarily studied, m3D6 (directed against an N-terminal domain of Abeta) and m266.2 (directed against the central domain of Abeta). Quantitative analysis of fibril formation was accomplished in several ways, including the determination of the number of fibrils per mum2 and by aggregate size analysis. These methods showed that both m3D6 and m266.2 significantly retarded the early stages of fibril formation.

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