[beta]-Amyloid (12-28)

Injection of the amyloid ?-protein fragment VHHQKLVFFAEDVGSNK into different limbic system structures in mice impaired retention with remarkably similar efficacy and in a dose-dependent manner. A? (12-28) and other A? fragments may exert dysregulatory cognitive effects by incoordination of K? channel function in neurons, glia and endothelial cells. A� (12�28) residues are the binding site for apolipoprotein E (apoE) on A�. This sequence encompasses a hydrophobic domain (residues 14�21) and a �-turn (residues 22�28) which place two hydrophobic domains of A� 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of A� peptides into fibrils. The secondary structure of A� (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of A� is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of A� pathology in Alzheimer�s disease (AD). A� (11-28) and five other fragments enhanced aggregation of full length A� (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length A�.

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