Amyloid fibrils in Alzheimer’s disease are composed of β-amyloid (Aβ) peptides of variant lengths. Humanin, HN (1-24), a neuroprotective peptide, is known to interact with the predominant Aβ isoform in the brain, Aβ (1-40), and prevent its aggregation. We employed molecular dynamics and density functional methods to identify residues that are important for both HN-HN and HN-Aβ interactions. Residues 7, 8, 11, and 18 in HN are involved in binding both to the 10-17 region of Aβ (1-40) in the heterodimer and in the homodimer. To further investigate the role of some of these residues, peptides corresponding to HN S14G, HN P19S, HN (5-15), HN (5-15, L11S), and Aβ (17-28) were investigated with respect to their ability to bind to Aβ (1-40).

Exploration of the Humanin-β-amyloid interaction using a combined molecular dynamics and quantum approach

256th National Meeting (2018)

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