The adsorption of amyloidogenic peptides, amyloid beta 1-40 (Aβ1-40), alpha-synuclein (α-syn), and beta 2 microglobulin (β2m), was attempted over the surface of nano-gold colloidal particles, ranging between 10 nm and 100 nm in diameter. The change in surface property caused by the degree of peptide coverage was hypothesized to reflect the coverage ratio (Θ) of amyloidogenic peptides over gold colloid. The geometric analysis and simulation of reproducing Θ was conducted by assuming a prolate shape of all amyloidogenic peptides. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted Θ values. The complex nano-size dependence of Θ was explained by available spacing between adjacent prolates. When the secondary layer was formed, Aβ1-40 and β2m possessed a higher affinity to a partially negative nano-gold colloidal surface. On the other hand, α-syn peptides tend to interact each other.

Networking of amyloidogenic peptides over nano-gold colloidal particles’ surfaces

2019 Fall National Meeting

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