%0 Journal Article %1 francsmonerris2021microscopic %A Francés-Monerris, Antonio %A García-Iriepa, Cristina %A Iriepa, Isabel %A Hognon, Cécilia %A Miclot, Tom %A Barone, Giampaolo %A Monari, Antonio %A Marazzi, Marco %D 2021 %I The Royal Society of Chemistry %J Phys. Chem. Chem. Phys. %K covid-19 in_silico ivermectin %N 40 %P 22957-22971 %R 10.1039/D1CP02967C %T Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection %U http://dx.doi.org/10.1039/D1CP02967C %V 23 %X The identification of chemical compounds able to bind specific sites of the human/viral proteins involved in the SARS-CoV-2 infection cycle is a prerequisite to design effective antiviral drugs. Here we conduct a molecular dynamics study with the aim to assess the interactions of ivermectin, an antiparasitic drug with broad-spectrum antiviral activity, with the human Angiotensin-Converting Enzyme 2 (ACE2), the viral 3CLpro and PLpro proteases, and the viral SARS Unique Domain (SUD). The drug/target interactions have been characterized in silico by describing the nature of the non-covalent interactions found and by measuring the extent of their time duration along the MD simulation. Results reveal that the ACE2 protein and the ACE2/RBD aggregates form the most persistent interactions with ivermectin, while the binding with the remaining viral proteins is more limited and unspecific.

@article{francsmonerris2021microscopic, abstract = {The identification of chemical compounds able to bind specific sites of the human/viral proteins involved in the SARS-CoV-2 infection cycle is a prerequisite to design effective antiviral drugs. Here we conduct a molecular dynamics study with the aim to assess the interactions of ivermectin{,} an antiparasitic drug with broad-spectrum antiviral activity{,} with the human Angiotensin-Converting Enzyme 2 (ACE2){,} the viral 3CLpro and PLpro proteases{,} and the viral SARS Unique Domain (SUD). The drug/target interactions have been characterized in silico by describing the nature of the non-covalent interactions found and by measuring the extent of their time duration along the MD simulation. Results reveal that the ACE2 protein and the ACE2/RBD aggregates form the most persistent interactions with ivermectin{,} while the binding with the remaining viral proteins is more limited and unspecific.}, added-at = {2021-12-03T16:12:45.000+0100}, author = {Francés-Monerris, Antonio and García-Iriepa, Cristina and Iriepa, Isabel and Hognon, Cécilia and Miclot, Tom and Barone, Giampaolo and Monari, Antonio and Marazzi, Marco}, biburl = {https://www.bibsonomy.org/bibtex/25af8d17ed688637785647f704b72a957/fordham1}, description = {Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection - Physical Chemistry Chemical Physics (RSC Publishing)}, doi = {10.1039/D1CP02967C}, interhash = {669e3187afaa7b00a0bc18320765551a}, intrahash = {5af8d17ed688637785647f704b72a957}, journal = {Phys. Chem. Chem. Phys.}, keywords = {covid-19 in_silico ivermectin}, number = 40, pages = {22957-22971}, publisher = {The Royal Society of Chemistry}, timestamp = {2021-12-03T17:28:38.000+0100}, title = {Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection}, url = {http://dx.doi.org/10.1039/D1CP02967C}, volume = 23, year = 2021 }