Submission Type
Poster
Abstract
Earlier this year, Professor Yokoyama published a paper in the Langmuir Journal, "Protein Corona Formation and Aggregation Process of Amyloid Beta 1-40 Coated Gold Nano-Colloids". Together with my groupmate for this project, we further investigated the findings from this publication. We found that more different nano sizes of gold colloids followed the same trend when alternating between acidic and basic pH. This was done by using the imaging technique known as Surface Enhanced Raman Scattering (SERS) on Amyloid-beta1-40(Aβ1-40)proteins that had been coated with gold colloids (20 nanometers and 80 nanometers) to make a visual representation of the spectrum generated during the cluster formation, known as the aggregation process. The SERS spectrum as a function of the concentration of the inserted Aβ1-40showed evidence to suggest that the induction of adsorption, the process in which the proteins hold the gold colloids as a thin film, is nano-size dependent. In addition, the SERS analysis suggested that in the gold particles measuring 20 nanometers, the area of contact appeared to be relatively smaller by the existence of a C=C or -C-N bond of a histidine amino acid. Meanwhile, the gold particles measuring 80 nanometers suggested that the orientation of the benzene ring of either phenylalanine or tyrosine may have a significant role. However, regardless of the sizes of the particles investigated, the data analysis suggested that the β-sheet and the random coil of polymer conformations had a significant influence on the gold colloid aggregation process.
Recommended Citation
Martinez Hernandez, Bryan, "246-Amyloid Beta 1-40 Protein Corona Formation on Gold Colloids and Investigation of Nano-size Dependence" (2024). GREAT Day Posters. 68.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2024/posters-2024/68
246-Amyloid Beta 1-40 Protein Corona Formation on Gold Colloids and Investigation of Nano-size Dependence
Earlier this year, Professor Yokoyama published a paper in the Langmuir Journal, "Protein Corona Formation and Aggregation Process of Amyloid Beta 1-40 Coated Gold Nano-Colloids". Together with my groupmate for this project, we further investigated the findings from this publication. We found that more different nano sizes of gold colloids followed the same trend when alternating between acidic and basic pH. This was done by using the imaging technique known as Surface Enhanced Raman Scattering (SERS) on Amyloid-beta1-40(Aβ1-40)proteins that had been coated with gold colloids (20 nanometers and 80 nanometers) to make a visual representation of the spectrum generated during the cluster formation, known as the aggregation process. The SERS spectrum as a function of the concentration of the inserted Aβ1-40showed evidence to suggest that the induction of adsorption, the process in which the proteins hold the gold colloids as a thin film, is nano-size dependent. In addition, the SERS analysis suggested that in the gold particles measuring 20 nanometers, the area of contact appeared to be relatively smaller by the existence of a C=C or -C-N bond of a histidine amino acid. Meanwhile, the gold particles measuring 80 nanometers suggested that the orientation of the benzene ring of either phenylalanine or tyrosine may have a significant role. However, regardless of the sizes of the particles investigated, the data analysis suggested that the β-sheet and the random coil of polymer conformations had a significant influence on the gold colloid aggregation process.