Submission Type
Poster
Start Date
4-21-2022
Abstract
The conformation of three amyloidogenic peptides; amyloid beta 1–40 (Aβ1−40), alpha synuclein (α-syn), and beta-2-microglobulin (β2m) are closely associated with the process of causing neurodegenerative diseases. Use of a peptide adsorbed gold nano-particle system allowed us to investigate the interactive segment of each peptide responsible for peptide-peptide networking, which is crucial to initiate the formation of an oligomer and leads to fibrillogenesis. The adsorption orientation of the amyloidogenic peptides on the nano-gold colloid spherical surface was explained by simulating how much area of the metal surface was covered by the peptides.The nano size dependence of Θ was linearly correlated with available spacing between adjacent peptides, Sd, which were approximated as prolates, For Aβ1−40 and α-syn, the 2nd layer was more included as Sdincreased. In contrast, β2m was found to gyrate over the gold surface as Sdincreased, creating a partially positive (δ+) region and repelling the extra β2m from the surface. Based on the trend found in an experimentally extracted Θ as a function of Sd, optimized charge distribution of Aβ1−40 and α-syn were concluded to be negative partial charge (δ−) region that was covered by the positive partial charge (δ+) region. However, β2m may have a relatively large and/or distributed δ+ region with a small portion of δ− at the one end of a prolate. The characterization made in this work confirmed current understandings on the formation of the protein corona over nano-particles.
Recommended Citation
Afonso, Stephanie; Benton, Emily; Wynne, Emily; and Carillo Rubio, Luis, "200 -- A Model for Nano-Scale Spherical Surface Coverage and Protein Corona Formation By Amyloidogenic Peptides" (2022). GREAT Day Posters. 66.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2022/posters-2022/66
200 -- A Model for Nano-Scale Spherical Surface Coverage and Protein Corona Formation By Amyloidogenic Peptides
The conformation of three amyloidogenic peptides; amyloid beta 1–40 (Aβ1−40), alpha synuclein (α-syn), and beta-2-microglobulin (β2m) are closely associated with the process of causing neurodegenerative diseases. Use of a peptide adsorbed gold nano-particle system allowed us to investigate the interactive segment of each peptide responsible for peptide-peptide networking, which is crucial to initiate the formation of an oligomer and leads to fibrillogenesis. The adsorption orientation of the amyloidogenic peptides on the nano-gold colloid spherical surface was explained by simulating how much area of the metal surface was covered by the peptides.The nano size dependence of Θ was linearly correlated with available spacing between adjacent peptides, Sd, which were approximated as prolates, For Aβ1−40 and α-syn, the 2nd layer was more included as Sdincreased. In contrast, β2m was found to gyrate over the gold surface as Sdincreased, creating a partially positive (δ+) region and repelling the extra β2m from the surface. Based on the trend found in an experimentally extracted Θ as a function of Sd, optimized charge distribution of Aβ1−40 and α-syn were concluded to be negative partial charge (δ−) region that was covered by the positive partial charge (δ+) region. However, β2m may have a relatively large and/or distributed δ+ region with a small portion of δ− at the one end of a prolate. The characterization made in this work confirmed current understandings on the formation of the protein corona over nano-particles.
Comments
Sponsored by Kazushige Yokoyama