Submission Type

Poster

Abstract

SARS-CoV-2 is protected by a viral membrane which requires a viral capsid to fuse with a cell as an initial step in the infection process. This fusion process utilizes glycoproteins on the surface of the viral membrane to interact with cell surface proteins to help catalyze membrane fusion. The lipid-bilayer enveloped virus protects the RNA inside, while the glycoprotein (s-protein) attached outside of the envelope initiates the cellular infection process. As for the case of SARS-CoV-2, an s-protein is highly associated with priming the viral infection. This project aimed to utilize the structural component of SARS-CoV-2 binding adsorbed to gold nanoparticles to further characterize the protein interaction dynamics by changing the concentration of protein added. We examined the shift of the Surface Plasmon Resonance (SPR) band of SARS-CoV-2 coated nano-gold colloids as a function of the change of an external pH by utilizing a UV-Vis Spectrophotometer. The pH of the solution was set to be around pH 3 by inserting pre-tested volumes of hydrochloric acid (HCl). Raman spectra are being collected using a WITec Raman alpha300R (WITec, GmbH) confocal Raman imaging system to study the protein’s conformation. Our group found that there is a relationship between the concentration of protein added and the amount of aggregation observed at an acidic pH, with a slight increase in pH as aggregation occurred.

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324-Spike Protein pH Hop Investigation of Protein Concentration

SARS-CoV-2 is protected by a viral membrane which requires a viral capsid to fuse with a cell as an initial step in the infection process. This fusion process utilizes glycoproteins on the surface of the viral membrane to interact with cell surface proteins to help catalyze membrane fusion. The lipid-bilayer enveloped virus protects the RNA inside, while the glycoprotein (s-protein) attached outside of the envelope initiates the cellular infection process. As for the case of SARS-CoV-2, an s-protein is highly associated with priming the viral infection. This project aimed to utilize the structural component of SARS-CoV-2 binding adsorbed to gold nanoparticles to further characterize the protein interaction dynamics by changing the concentration of protein added. We examined the shift of the Surface Plasmon Resonance (SPR) band of SARS-CoV-2 coated nano-gold colloids as a function of the change of an external pH by utilizing a UV-Vis Spectrophotometer. The pH of the solution was set to be around pH 3 by inserting pre-tested volumes of hydrochloric acid (HCl). Raman spectra are being collected using a WITec Raman alpha300R (WITec, GmbH) confocal Raman imaging system to study the protein’s conformation. Our group found that there is a relationship between the concentration of protein added and the amount of aggregation observed at an acidic pH, with a slight increase in pH as aggregation occurred.

 

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