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Research advance| March 30
Cell Research published the latest research on the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain. That leads to SARS-CoV-2 showed a superior plasma membrane fusion capacity compared to that of SARS-CoV.
More importantly, they the researchers generated a series of lipopeptides derived from EK1 (the optimized form of OC43-HR2P, showed substantially improved pan-CoV fusion inhibitory activity and pharmaceutical properties) and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection. learn more