Amyroid fibril is one of the causative agents of Alzheimer's disease and its structure and amyloidosis behavior is a major interesting of the researchers. Some kinds of protofilaments are precursors of the amyloid fibril, and they were usually made with oligo peptides. The structure and physical properties of the protofilaments should be related with amyloid forming, and its fundamental study should lead to reveal the amyloidosis behavior. We prepared 2 model peptides for the unit of proto filament. They had a part of Ovalbumin sequence that could form �-sheet structure, and one of them was combined with polyethylene glycol and the other was combined with TAT sequence. We carried out CD measurements, and we found the protofilaments contained �-sheet structure, that means the protofilament also took laminated structure as same as general amyloid fibril did. From the study of the X-ray scattering, the protofilaments took rod-like shape, and we found its cross section was rectangular shape rather than round shape (see figure 1, solid line shows theoretical curve of the rectangular rods). That is reasonable for the laminated structure of �-Sheets, and the layer number was calculated as 4 from the width of the rectangle.

Structural analysis of the protofilaments as units of amyroid fibril by SAXS

248th National Meeting (2014)

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