Submission Type
Poster
Start Date
April 2020
Abstract
The simulation of a peptide coverage was conducted by assuming a prolate shape of all amyloidogenic peptides taking a spiking-out orientation. In order to reproduce the extracted peptide coverage ratio, the involvement of a secondary layer was suggested. The secondary layer was considered to be due to the networking of the peptides. Both Ab1-40 and B2M are considered to have a partial charge (+) distribution centering around the prolate axis. The a-syn, on the other hand, possesses a distorted charge distribution. For relatively lower coverage (< 0.56), a prolate was assumed to conduct a gyration motion, maintaining the spiking-out orientation in order to fill in the unoccupied space with a tilting angle of approximately 30o.
Recommended Citation
Ichiki, Akane, "352— Determination of nano-scale adsorption orientation of peptide" (2020). GREAT Day Posters. 11.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2020/posters-2020/11
352— Determination of nano-scale adsorption orientation of peptide
The simulation of a peptide coverage was conducted by assuming a prolate shape of all amyloidogenic peptides taking a spiking-out orientation. In order to reproduce the extracted peptide coverage ratio, the involvement of a secondary layer was suggested. The secondary layer was considered to be due to the networking of the peptides. Both Ab1-40 and B2M are considered to have a partial charge (+) distribution centering around the prolate axis. The a-syn, on the other hand, possesses a distorted charge distribution. For relatively lower coverage (< 0.56), a prolate was assumed to conduct a gyration motion, maintaining the spiking-out orientation in order to fill in the unoccupied space with a tilting angle of approximately 30o.
Comments
Sponsored by Kazushige Yokoyama