Submission Type
Poster
Start Date
4-26-2021
Abstract
Gold nano-particles were coated with the spike protein (S protein) of SARS-CoV-2 and exposed to increasingly acidic conditions. Their responses were investigated by monitoring the surface plasmon resonance (SPR) band shift. As the external pH was gradually changed from neutral pH to pH ~2 the peak of the SPR band showed a significant red-shift, with a sigmoidal feature implying the formation of the gold-protein aggregates. The coating of S protein changed the surface property of the gold enough to extract the coverage fraction of protein over nano particles, Θ, which did not exhibit clear nanosize dependence. The geometrical simulation to explain Θ showed the average axial length to be a = 7. 25 nm and b =8.00 nm when the Sprotein was hypothesized as a prolate shape with spiking-out orientation. As the pH value externally hopped between pH~3 and pH~10, a behavior of reversible protein folding was observed for particles with diameters >30 nm. It was concluded that S protein adsorption conformation was impacted by the size (diameter, d) of a core nano-gold, where head-to-head dimerized S protein was estimated for d ≤ 80 nm and a parallel in opposite directions formation for d = 100 nm.
Recommended Citation
Lin, Zi Chao, "065— Nano-size Dependence in the Adsorption by the SARS-CoV-2 Spike Protein Over Gold Colloid" (2021). GREAT Day Posters. 29.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2021/posters-2021/29
065— Nano-size Dependence in the Adsorption by the SARS-CoV-2 Spike Protein Over Gold Colloid
Gold nano-particles were coated with the spike protein (S protein) of SARS-CoV-2 and exposed to increasingly acidic conditions. Their responses were investigated by monitoring the surface plasmon resonance (SPR) band shift. As the external pH was gradually changed from neutral pH to pH ~2 the peak of the SPR band showed a significant red-shift, with a sigmoidal feature implying the formation of the gold-protein aggregates. The coating of S protein changed the surface property of the gold enough to extract the coverage fraction of protein over nano particles, Θ, which did not exhibit clear nanosize dependence. The geometrical simulation to explain Θ showed the average axial length to be a = 7. 25 nm and b =8.00 nm when the Sprotein was hypothesized as a prolate shape with spiking-out orientation. As the pH value externally hopped between pH~3 and pH~10, a behavior of reversible protein folding was observed for particles with diameters >30 nm. It was concluded that S protein adsorption conformation was impacted by the size (diameter, d) of a core nano-gold, where head-to-head dimerized S protein was estimated for d ≤ 80 nm and a parallel in opposite directions formation for d = 100 nm.
Comments
Sponsored by Yokoyama Kazushige. Selected for presentation at the American Chemical Society National Meeting