Aß (12–28) residues are the binding site for apolipoprotein E (apoE) on Aß. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Aß (11-28) and five other fragments enhanced aggregation of full length Aß (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 Aß.
Sadowski, M. et al. Am. J. Pathol. 165, 937 (2004); Liu, R. et al. J. Neurosci. Res. 75, 162 (2004).
Sequence (One-Letter Code)
Sequence (Three-Letter Code)
H - Val - His - His - Gln - Lys - Leu - Val - Phe - Phe - Ala - Glu - Asp - Val - Gly - Ser - Asn - Lys - OH