P2–062: Binding of cholesterol to the C99 domain of APP competes with homodimerzation of the protein

AApeptide and also their potential on anti-Alzheimer’s diseases was evaluated.Methods: Herein, one bead one compound AApeptide library was designed for the selection of ligand that targets on Abeta. Selected AApeptides was evaluated for their effect on Aß1-40monomer peptides in their progress of aggregation. Methods are listed as follows: 1. Thioflavin T assay, ß-sheet formation assay for anti-aggregation screening. 2. TEM assay was used to image the morphological change of Aß fibrils with/without presence of AApeptide. 3. Western Blot, in vitro aggregation of HFIP treated Aß1-40 was produced to aggregate under room temperature, theformation of oligomers were detected using 6E10 anti-Aß antibodies. Following LI-COR western was used and quantification was performed for evaluation. Tissue culture, MTT assay on Neuroblastoma cell to test their toxicity. Kit using commercial available methods from Roche. Results: One of screened AApeptides shows great potential of anti-aggregation at concentration of 2.5mM at 1:1 ratio with Abeta. TEM assay also confirmed clearance of Aß fibrils in the presence of AApeptide. Toxicity of neuroblastma cells of AApeptide is not obvious at effective concentration. Conclusions: As a new generation of peptidomimetics, short AApeptide has great potential on Anti-Alzheimer’s diseases as an anti-aggregation drug.