TY - JOUR
T1 - Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2
T2 - A computational and biophysical approach
AU - González-Paz, Lenin
AU - Hurtado-León, María Laura
AU - Lossada, Carla
AU - Fernández-Materán, Francelys V.
AU - Vera-Villalobos, Joan
AU - Loroño, Marcos
AU - Paz, J. L.
AU - Jeffreys, Laura
AU - Alvarado, Ysaias J.
N1 - Publisher Copyright:
© 2021 Elsevier B.V.
PY - 2021/11
Y1 - 2021/11
N2 - The SARS-CoV-2 pandemic has accelerated the study of existing drugs. The mixture of homologs called ivermectin (avermectin-B1a [HB1a] + avermectin-B1b [HB1b]) has shown antiviral activity against SARS-CoV-2 in vitro. However, there are few reports on the behavior of each homolog. We investigated the interaction of each homolog with promising targets of interest associated with SARS-CoV-2 infection from a biophysical and computational-chemistry perspective using docking and molecular dynamics. We observed a differential behavior for each homolog, with an affinity of HB1b for viral structures, and of HB1a for host structures considered. The induced disturbances were differential and influenced by the hydrophobicity of each homolog and of the binding pockets. We present the first comparative analysis of the potential theoretical inhibitory effect of both avermectins on biomolecules associated with COVID-19, and suggest that ivermectin through its homologs, has a multiobjective behavior.
AB - The SARS-CoV-2 pandemic has accelerated the study of existing drugs. The mixture of homologs called ivermectin (avermectin-B1a [HB1a] + avermectin-B1b [HB1b]) has shown antiviral activity against SARS-CoV-2 in vitro. However, there are few reports on the behavior of each homolog. We investigated the interaction of each homolog with promising targets of interest associated with SARS-CoV-2 infection from a biophysical and computational-chemistry perspective using docking and molecular dynamics. We observed a differential behavior for each homolog, with an affinity of HB1b for viral structures, and of HB1a for host structures considered. The induced disturbances were differential and influenced by the hydrophobicity of each homolog and of the binding pockets. We present the first comparative analysis of the potential theoretical inhibitory effect of both avermectins on biomolecules associated with COVID-19, and suggest that ivermectin through its homologs, has a multiobjective behavior.
KW - Avermectin
KW - COVID-19
KW - Ivermectin
KW - Molecular docking
KW - Molecular dynamic
KW - SARS-CoV-2
UR - http://www.scopus.com/inward/record.url?scp=85113601480&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2021.106677
DO - 10.1016/j.bpc.2021.106677
M3 - Artículo
AN - SCOPUS:85113601480
SN - 0301-4622
VL - 278
JO - Biophysical Chemistry
JF - Biophysical Chemistry
M1 - 106677
ER -