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The study aims to express and purify the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein using recombinant protein techniques and evaluate its binding affinity to the human ACE2 receptor. HEK293T cells were transfected with two plasmids: one expressed RBD fused with a His-tag allowing protein purification via immobilized metal affinity chromatography (IMAC) and the other expressed RBD fused with an sfGFP-tag allowing fluorescence detection of protein expression. Purification of the recombinant His-tagged RDB and sfGFP-tagged RBD protein products using IMAC, Hydrophobic interaction chromatography (HIC) and Ion exchange chromatography is ongoing. BCA protein assay, SDS-PAGE, Western blotting, and ELISA will be performed to assess expression yield, purity, and binding interactions. The research enhances understanding of the effects of two common tags on SARS-CoV-2 RBD dynamics and their potential applications in diagnostics, therapeutics, and vaccine development against COVID-19.
