RT info:eu-repo/semantics/article
T1 Computational study on the affinity of potential drugs to SARS-CoV-2 main protease
A1 Martín, Verónica
A1 Sanz Novo, Miguel
A1 León Ona, Iker
A1 Redondo Cristóbal, María del Pilar
A1 Largo Cabrerizo, Antonio
A1 Barrientos Benito, María Carmen
A1 sanz, m
K1 molecular docking
K1 dexamethasone
K1 betamethasone
K1 chloroquine
K1 hydroxychloroquine
K1 SARS-CoV-2 main protease
AB Herein, we report a computational investigation of the binding affinity of dexamethasone,betamethasone, chloroquine and hydroxychloroquine to SARS-CoV-2 main proteaseusing molecular and quantum mechanics as well as molecular docking methodologies. We aimto provide information on the anti-COVID-19 mechanism of the abovementioned potentialdrugs against SARS-CoV-2 coronavirus. Hence, the 6w63 structure of the SARS-CoV-2main protease was selected as potential target site for the docking analysis. The studyincludes an initial conformational analysis of dexamethasone, betamethasone, chloroquine andhydroxychloroquine. For the most stable conformers, a spectroscopic analysis has been carriedout. In addition, global and local reactivity indexes have been calculated to predict the chemicalreactivity of these molecules. The molecular docking results indicate that dexamethasoneand betamethasone have a higher affinity than chloroquine and hydroxychloroquinefor their theoretical 6w63 target. Additionally, dexamethasone and betamethasoneshow a hydrogen bond with the His41 residue of the 6w63 protein, while the interactionbetween chloroquine and hydroxychloroquine with this amino acid is weak. Thus, we confirmthe importance of His41 amino acid as a target to inhibit the SARS-CoV-2 Mpro activity.
PB IOP Publishing
SN 0953-8984
YR 2022
FD 2022
LK https://uvadoc.uva.es/handle/10324/65260
UL https://uvadoc.uva.es/handle/10324/65260
LA spa
NO Journal of Physics: Condensed Matter, Volume 34, Number 29
NO Producción Científica
DS UVaDOC
RD 22-dic-2024