jp9b07359_si_001.pdf (1.19 MB)
Surface Inhomogeneity of Graphene Oxide Influences Dissociation of Aβ16–21 Peptide Assembly
journal contribution
posted on 2019-10-17, 18:41 authored by Zhi He, Jingyuan Li, Serena H. Chen, Ruhong ZhouAbnormal
peptide assembly and aggregation is associated with an
array of neurodegenerative diseases including Alzheimer’s disease
(AD). A detailed understanding of how nanostructured materials such
as oxidized graphene perturb the peptide assembly and subsequently
induce fibril dissociation may open new directions for the development
of potential AD treatments. Here, we investigate the impact of surface
inhomogeneity of graphene oxide (GO) on the assembly of amyloid-beta
Aβ16–21 peptides on GO surfaces with different
degrees of oxidation using molecular dynamics simulations. Interestingly,
nonuniform GO nanosheets (in terms of oxidation sites) have a much
stronger perturbation effect on the structure of Aβ16–21 assembly. The Aβ peptides exhibit a remarkable tendency in
binding to the scattered interfaces between unoxidized and oxidized
regions, which induces the dissociation of Aβ amyloid fibril.
These findings should deepen our understanding of surface-induced
peptide dissociation and stimulate discovery of alternative AD treatments.