The adsorption orientation of amyloidogenic peptides, amyloid beta 1-40 (Aβ1-40), alpha-synuclein (α-syn), and beta 2 microglobulin (β2m), was investigated by geometrical simulation which was developed in our group. Empirically extracted peptide coverage ratio (Θ) of amyloidogenic peptides over gold colloid was utilized to identify not only adsorption orientation but also plausible sequence, which is a core of the adsorption. The geometric simulation of reproducing Θ was conducted by assuming each to be prolate of different size. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted Θ values for many cases. In some cases, lie-down orientation was found to be the best suited orientation. However, this lie-down orientation was explained as a result of a gyration of a prolate with spiking-out orientation. The nano-size dependence of Θ was not straightforward though, geometrical analysis explained that nano-dependence was due to an available spacing between adjacent prolates. When the secondary layer was formed, Aβ1-40 and α-syn tend to invite in another peptide to the gold surface as they possess more adjacent distances. However, an adsorbed β2m monomer tends to invite more monomers as the adjacent distance becomes shorter. This difference implies the difference of peptide conformation and charge distribution.

Investigation of an adsorption orientation of amyloidogenic peptides over nano-gold colloidal particles’ surfaces and peptide-peptide networking

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.