Interaction of the new inhibitor paxlovid (PF-07321332) and ivermectin with the monomer of the main protease SARS-CoV-2: A volumetric study based on molecular dynamics, elastic networks, classical thermodynamics and SPT
Ysaias José Alvarado, Yosmari Olivarez, Carla Lossada, Joan Vera-Villalobos, José Luis Paz, Eddy Vera, Marcos Loroño, Alejandro Vivas, Fernando Javier Torres, María Laura N Jeffreys, María Laura Hurtado-León, Lenin González-Paz
Computational Biology and Chemistry, doi:10.1016/j.compbiolchem.2022.107692
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Under this same study strategy, it was found that PF-07321332 can also covalently bind to another region of the monomer (a drug multi-site for M pro ), but both complexes have similar structural flexibility and volumetric properties. Finally, we consider that this type of study can help to understand the mechanism by which a ligand can block the homodimerization of this important monomer to form the dimeric protease dM pro and in turn help in studies of activity-structure relationships for the design of new drugs.
Declaration of competing interest. The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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