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Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection
Francés-Monerris et al., Physical Chemistry Chemical Physics, doi:10.1039/D1CP02967C
Francés-Monerris et al., Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection, Physical Chemistry Chemical Physics, doi:10.1039/D1CP02967C
Oct 2021   Source   PDF  
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In Silico molecular dynamics study showing that ACE2 and ACE2/RBD aggregates form persistent interactions with ivermectin.
Francés-Monerris et al., 5 Oct 2021, peer-reviewed, 8 authors.
In Silico studies are an important part of preclinical research, however results may be very different in vivo.
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Abstract: PCCP View Article Online PAPER Published on 05 October 2021. Cite this: Phys. Chem. Chem. Phys., 2021, 23, 22957 View Journal | View Issue Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection† Antonio Francés-Monerris, *ab Cristina Garcı́a-Iriepa, Cécilia Hognon, a Tom Miclot,af Giampaolo Barone, and Marco Marazzi *cd f *cd Isabel Iriepa, Antonio Monari ce *ag 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 Received 30th June 2021, Accepted 4th October 2021 drug/target interactions have been characterized in silico by describing the nature of the non-covalent DOI: 10.1039/d1cp02967c 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 rsc.li/pccp ivermectin, while the binding with the remaining viral proteins is more limited and unspecific.
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