Non-conventional interactions of N3 inhibitor with the main protease of SARS-CoV and SARS-CoV-2


Por: Garcia-Gutierrez, Ponciano, Zubillaga, Rafael A., Ibarra, Ilich A., Martinez, Ana, Vargas, Rubicelia, Garza, Jorge

Publicada: 1 ene 2021
Resumen:
The extensive spread of COVID-19 in every continent shows that SARS-CoV-2 virus has a higher transmission rate than SARS-CoV virus which emerged in 2002. This results in a global pandemic that is difficult to control. In this investigation, we analyze the interaction of N3 inhibitor and the main protease of SARS-CoV and SARS-CoV-2 by quantum chemistry calculations. Non-covalent interactions involved in these systems were studied using a model of 469 atoms. Density Functional Theory and Quantum Theory of Atoms in Molecules calculations lead us to the conclusion that non-conventional hydrogen bonds are important to describe attractive interactions in these complexes. The energy of these non-conventional hydrogen bonds represents more than a half of the estimated interaction energy for non-covalent contacts. This means that hydrogen bonds are crucial to correctly describe the bonds between inhibitors and the main proteases. These results could be useful for the design of new drugs, since non-covalent interactions are related to possible mechanisms of action of molecules used against these viruses. (C) 2021 Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.

Filiaciones:
Departamento de Química, División de Ciencias Básicas e Ingeniería, Universidad Autónoma Metropolitana-Iztapalapa, San Rafael Atlixco 186, Col. Vicentina, Iztapalapa, Ciudad de México 09340, Mexico
Instituto de Investigaciones en Materiales, Universidad Nacional Autónoma de México, Circuito Exterior S. N., Ciudad Universitaria, Coyoacán, Ciudad de México 04510, Mexico
ISSN: 20010370





Computational and Structural Biotechnology Journal
Editorial
Elsevier, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, Suecia
Tipo de documento: Article
Volumen: 19 Número:
Páginas: 4669-4675
WOS Id: 000694712900006
ID de PubMed: 34401047
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