(489.8) Synthesis of the transmembrane domain of the accessory protein ORF7a of SARS-CoV-2 using solid phase peptide synthesis and analyzing the oligomerization state

Poster Board Number: A78

Tyler Hobart (Hampden-Sydney College), Timothy Reichart (Hampden-Sydney College)

This research project consists of synthesizing and characterizing the accessory protein ORF7a of SARS-CoV-2. ORF7a plays a role in viral assembly and inhibition of this protein would prevent viruses from assembling and spreading within a host’s cells. The goal of this project is to determine the oligomerization state of the protein through a fluorescence assay, which would determine the protein’s structure and how it folds. After determining the oligomerization state of the protein, potential inhibitors could be synthesized and tested for their efficacy at inhibiting the function of the protein. Synthesis of the protein was done using a solid phase peptide synthesis technique. Characterization and purification were done using High Performance Liquid Chromatography (HPLC) as well as Liquid Chromatography Mass Spectrometry (LCMS). Fluorescence assay was performed using a UV-vis spectrometer. This presentation will highlight current progress with the oligomerization state with the goal of devising an effective inhibitor for ORF7 activity in SARS-CoV-2 particle assembly.

Support or Funding Information

Hampden-Sydney College Office of Undergraduate Research