The geometric analysis and simulation of three amyloidogenic peptides: Amyloid beta  1-40 (Aβ<sub>1-40</sub>), Beta 2 myoglobin (β2m), and Alpha-synuclein (α-syn) were calculated. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted peptide coverage ratio, Θ. The involvement of a secondary layer was suggested due to the networking of the three peptides. Both Aβ<sub>1-40</sub> and β2m were considered to have a partial positive charge distribution centering around the prolate axis. However, the α-syn possessed a distorted charge distribution. When α-syn has a relatively lower Θ (i.e., Θ &lt; 0.56), a prolate was assumed to conduct a gyration motion, which maintains the spiking-out orientation in order to fill in the unoccupied space with a tilting angle of approximately 25°.

Determination of the nano-scale adsorption orientation of amyloidogenic peptides

2019 Fall National Meeting

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