SYNTHESIS OF β-SHEET-TERMINATER WITH A VIEW TO DEVELOPING MEDICAL THERAPY FOR ALZHEIMER'S DISEASE

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Amphiphilic molecules that contain a tripeptide moiety form an aggregate not only in water but also in organic solvents. The aggregate possesses fibrous morphology and involves a rich amount of parallel β-sheet structure of peptides, which is similar to a β-peptide called an amyloid fibril. These similarities suggest that the tripeptide containing amphiphiles are suitable for an amyloid model. In the present study, we attempted to disintegrate the β-sheet assemblage by addition of a terminator molecule that lacked two proton donors for the interpeptide H-bonding. Aggregation of a tripeptide-containing amphiphile is accompanied by gel formation. The organogel turned into a light solution by addition of the terminator molecule.