Synthesis and Analysis of the SARS-CoV-2 ORF7a Accessory Protein Transmembrane Domain and Determination of the Oligomerization State
Journal of Biological Chemistry
; 299(3 Supplement):S84, 2023.
Artigo
em Inglês
| EMBASE | ID: covidwho-20236838
ABSTRACT
The ongoing SARS-CoV-2 pandemic continues to sicken millions worldwide and fundamentally change the way people interact with each other. In order to better characterize the SARS-CoV-2 virus and potentially develop methods of inhibition for further spread of the disease, this research project focused on synthesizing and characterizing the trans-membrane region of the accessory protein ORF7a. ORF7a has been implicated in proper viral assembly, leading to the idea that inhibition of this protein could prevent viral copies from being produced and halt the spread of the virus. The goal of this project was to determine the oligomerization state of the protein through a fluorescence assay in order to better understand the quaternary structure of the ORF7a complex and how it folds. The fluorescence assay is performed using three different samples of the synthesized peptide one labeled with a TAMRA fluorophore, one labeled with a NBD fluorophore, and the last is unlabeled. 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. Further applications of these inhibitors on other viruses can be explored due to the highly conserved nature of transmembrane domains across multiple viral families. Synthesis of the protein was done using a Solid Phase Peptide Synthesis (SPPS) technique and multiple batches of all three samples of peptide have been generated. Characterization and purification were done using High Performance Liquid Chromatography (HPLC) as well as Liquid Chromatography Mass Spectrometry (LCMS). Current research focuses on the purification and quantification of purified ORF7a oligopeptide for implementation of the fluorescence assay. -Hampden-Sydney College Office of Undergraduate Research.Copyright © 2023 The American Society for Biochemistry and Molecular Biology, Inc.
case report; clinical article; conference abstract; drug efficacy; fluorescence analysis; high performance liquid chromatography; human; liquid chromatography-mass spectrometry; nonhuman; oligomerization; peptide synthesis; protein domain; protein function; protein quaternary structure; protein synthesis; Severe acute respiratory syndrome coronavirus 2; solid; synthesis; virus assembly; endogenous compound; oligopeptide
Texto completo:
Disponível
Coleções:
Bases de dados de organismos internacionais
Base de dados:
EMBASE
Idioma:
Inglês
Revista:
Journal of Biological Chemistry
Ano de publicação:
2023
Tipo de documento:
Artigo
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