Student Hampden-Sydney College Spotsylvania, Virginia, United States
Alexander Washington (Hampden-Sydney College)| Timothy Reichart (Hampden-Sydney College)
The SARS-CoV-2 spike protein transmembrane (TM) domain is an important component of the protein that contributes to its oligomerization for its active configuration. An understanding of this function can yield valuable data to future research on how to inhibit the virus’ infection of a host. The TM region of the protein is not as well studied due to the complication that nonpolar peptides can have in large groups; therefore, an understanding of this region could lead to novel discoveries. A peptide of the TM domain must be synthesized by using Solid Phase Peptide Synthesis, in which a resin is utilized to build a peptide off the c-terminus using Fmoc-protected amino acids and a strong base. A fluorescence assay can be performed to determine its oligomerization state by looking at the change of fluorescence that occurs when a quencher is added to the solution. Once the oligomerization state of the spike proteins TM domain is determined, this information will be beneficial the development of drugs against the virus. The set up to run this synthesis was developed in the lab and is causing premature termination of the amino acid chain. Current work involves addressing a potential issue of hydrophobicity due to the volume non-polar residues, which is currently being address by trying a TGR resin that has a polystyrene core which is suited for long peptides. It is anticipated that addressing this issue will lead to a peptide that can be purified. The future implications of this research is that it has the potential of being useful for drugs that would inhibit the active configuration of SARS-CoV-2.