SARS-CoV-2 M < sup > pro < /sup > oligomerization as a potential target for therapy

In this study, we utilized biochemical, structural, and molecular modelling approaches to explore Mpro dimerization. We evaluated critical residues, specifically Arg4 and Arg298, that are essential for dimerization. Our results show that changes in the oligomerization state of Mpro directly affect its enzymatic activity and dimerization propensity. We discovered a synergistic relationship influencing dimer formation, involving both intra- and intermolecular interactions. These findings highlight the potential for developing allosteric inhibitors targeting Mpro, offering promising new directions for therapeutic strategies.PMID:38582483 | DOI:10.1016/j.ijbiomac.2024.131392
Source: International Journal of Biological Macromolecules - Category: Biochemistry Authors: Source Type: research