Molecular imaging ofAlzheimer amyloid

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This study aimed to develop and compare chemical compounds which bind amyloid structure in brains with Alzheimer's disease. We first started stylbene then flavone and aurone structures as potent ligands for amyloid imaging. We dedicated particularly to compare these compounds with PIB that is well established as the original compound developed by Pittsuberg University research group. All of these compounds mimic thioflavine as the mother structure and examined their high incorporation and exclusion from the brain tissue. One of the major problem was not to detect any positive signal of PIB for transgenic mice named Tg2576 although PIB demonstrated the beautiful imaging for patients with AD. We explored this base by comparison of two line of transgenic mice of APP23 and Tg2576 x PS 1 double transgenic mice. We first reproduced the negative signal for Tg2576 line but succeeded in detect the strong PIB signal for APP23. Then we compared both brain tissues after PET imaging. Both tissues show many amyloid plaques enough to be detected with amyloid antibodies. We examined tissues with several amyloid antibodies and finally reached to find one antibody to distinguish APP23 from Tg2576. This antibody was supposed to specifically recognize pyroglutamate at the third residue of amyloid protein. This post modification was originally found by me. The present result clearly explains the discrepancy between acceleration animal model and human aged patients with AD.