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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
Oct 2021  
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Ivermectin for COVID-19
4th treatment shown to reduce risk in August 2020
*, now known with p < 0.00000000001 from 102 studies, recognized in 22 countries.
No treatment is 100% effective. Protocols combine complementary and synergistic treatments. * >10% efficacy in meta analysis with ≥3 clinical studies.
4,000+ studies for 60+ treatments.
In Silico molecular dynamics study showing that ACE2 and ACE2/RBD aggregates form persistent interactions with ivermectin.
Ivermectin, better known for antiparasitic activity, is a broad spectrum antiviral with activity against many viruses including H7N7 Götz, Dengue Jitobaom, Tay, Wagstaff, HIV-1 Wagstaff, Simian virus 40 Wagstaff (B), Zika Barrows, Jitobaom, Yang, West Nile Yang, Yellow Fever Mastrangelo, Varghese, Japanese encephalitis Mastrangelo, Chikungunya Varghese, Semliki Forest virus Varghese, Human papillomavirus Li, Epstein-Barr Li, BK Polyomavirus Bennett, and Sindbis virus Varghese.
Ivermectin inhibits importin-α/β-dependent nuclear import of viral proteins Götz, Kosyna, Wagstaff, Wagstaff (B), inhibits SARS-CoV-2 3CLpro Mody, shows spike-ACE2 disruption at 1nM with microfluidic diffusional sizing Fauquet, binds to glycan sites on the SARS-CoV-2 spike protein preventing interaction with blood and epithelial cells and inhibiting hemagglutination Boschi, Scheim, exhibits dose-dependent inhibition of lung injury Abd-Elmawla, Ma, may inhibit SARS-CoV-2 via IMPase inhibition Jitobaom, may inhibit SARS-CoV-2 induced formation of fibrin clots resistant to degradation Vottero, may inhibit SARS-CoV-2 RdRp activity Parvez (B), may be beneficial for COVID-19 ARDS by blocking GSDMD and NET formation Liu (C), shows protection against inflammation, cytokine storm, and mortality in an LPS mouse model sharing key pathological features of severe COVID-19 DiNicolantonio, Zhang, may be beneficial in severe COVID-19 by binding IGF1 to inhibit the promotion of inflammation, fibrosis, and cell proliferation that leads to lung damage Zhao, may minimize SARS-CoV-2 induced cardiac damage Liu, Liu (B), increases Bifidobacteria which play a key role in the immune system Hazan, has immunomodulatory Munson and anti-inflammatory DiNicolantonio (B), Yan properties, and has an extensive and very positive safety profile Descotes.
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.
This PaperIvermectinAll
Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection
Antonio Francés-Monerris, Cristina García-Iriepa, Isabel Iriepa, Cécilia Hognon, Tom Miclot, Giampaolo Barone, Antonio Monari, Marco Marazzi
Physical Chemistry Chemical Physics, doi:10.1039/d1cp02967c
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 3CL pro and PL pro 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.
Conflicts of interest There are no conflicts to declare.
Ahmed, Karim, Ross, Hossain, Clemens et al., A five-day course of ivermectin for the treatment of COVID-19 may reduce the duration of illness, Int. J. Infect. Dis
Arafet, Serrano-Aparicio, Lodola, Mulholland, Gonza ´lez et al., Mechanism of inhibition of SARS-CoV-2 M pro by N3 peptidyl Michael acceptor explained by QM/MM simulations and design of new derivatives with tunable chemical reactivity, Chem. Sci
Are ´valo, Pagotto, Po ´rfido, Daghero, Segovia et al., Ivermectin reduces in vivo coronavirus infection in a mouse experimental model, Sci. Rep
Azam, Taban, Eid, Iqbal, Alam et al., An in-silico analysis of ivermectin interaction with potential SARS-CoV-2 targets and host nuclear importin a, J. Biomol. Struct. Dyn
Ba ´ez-Santos, Mielech, Deng, Baker, Mesecar, Catalytic function and substrate specificity of the papain-like protease domain of nsp3 from the Middle East respiratory syndrome coronavirus, J. Virol
Ba ´ez-Santos, St, John, Mesecar, The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds, Antiviral Res
Barros, Casalino, Gaieb, Dommer, Wang et al., The flexibility of ACE2 in the context of SARS-CoV-2 infection, Biophys. J
Be ´ke ´s, Ekkebus, Ovaa, Huang, Lima, Recognition of Lys48-linked di-ubiquitin and deubiquitinating activities of the SARS coronavirus papainlike protease, Mol. Cell
Becke, A new mixing of Hartree-Fock and local densityfunctional theories, J. Chem. Phys
Bedford, Enria, Giesecke, Heymann, Ihekweazu et al., COVID-19: towards controlling of a pandemic, Lancet
Behera, Patro, Singh, Chandanshive, Ravikumar et al., Role of ivermectin in the prevention of SARS-CoV-2 infection among healthcare workers in India: A matched case-control study, PLoS One
Bello, Elucidation of the inhibitory activity of ivermectin with host nuclear importin a and several SARS-CoV-2 targets, J. Biomol. Struct. Dyn
Bhardwaj, Singh, Das, Purohit, Evaluation of acridinedione analogs as potential SARS-CoV-2 main protease inhibitors and their comparison with repurposed anti-viral drugs, Comput. Biol. Med
Bhardwaj, Singh, Sharma, Rajendran, Purohit et al., Bioactive Molecules of Tea as Potential Inhibitors for RNA-Dependent RNA Polymerase of SARS-CoV-2, Front. Med
Bhardwaj, Singh, Sharma, Rajendran, Purohit et al., Identification of bioactive molecules from tea plant as SARS-CoV-2 main protease inhibitors, J. Biomol. Struct. Dyn
Caly, Druce, Catton, Jans, Wagstaff, The FDA-approved drug ivermectin inhibits the replication of SARS-CoV-2 in vitro, Antiviral Res
Case, Betz, Cerutti, Cheatham, Darden et al., None, Amber
Chaccour, Casellas, Blanco-Di Matteo, Pineda, Fernandez-Montero et al., The effect of early treatment with ivermectin on viral load, symptoms and humoral response in patients with non-severe COVID-19: A pilot, double-blind, placebo-controlled, randomized clinical trial, EClinicalMedicine
Chaccour, Hammann, Ramo ´n-Garcı ´a, Rabinovich, Ivermectin and COVID-19: keeping rigor in times of urgency, Am. J. Trop. Med. Hyg
Chang, Yan, Xie, Gao, Song et al., Different roles for two ubiquitin-like domains of ISG15 in protein modification, J. Biol. Chem
Choudhury, Das, Patra, Bhattacharya, Ghosh et al., Exploring the binding efficacy of ivermectin against the key proteins of SARS-CoV-2 pathogenesis: an in silico approach, Future Virol
Dasgupta, Sen, Bakshi, Dasgupta, Manna et al., Nsp7 and Spike Glycoprotein of SARS-CoV-2 are envisaged as Potential Targets of Vitamin D and Ivermectin, Preprints, doi:10.20944/preprints202005.0084.v1
Elmezayen, Al-Obaidi, S -Ahin, Yelekçi, Drug repurposing for coronavirus (COVID-19): in silico screening of known drugs against coronavirus 3CL hydrolase and protease enzymes, J. Biomol. Struct. Dyn
Eweas, Alhossary, Abdel-Moneim, Molecular Docking Reveals Ivermectin and Remdesivir as Potential Repurposed Drugs Against SARS-CoV-2, Front. Microbiol
Feller, Zhang, Pastor, Brooks, Constant pressure molecular dynamics simulation: The Langevin piston method, J. Chem. Phys
France ´s-Monerris, Hognon, Miclot, Garcı ´a-Iriepa, Iriepa et al., Molecular Basis of SARS-CoV-2 Infection and Rational Design of Potential Antiviral Agents: Modeling and Simulation Approaches, J. Proteome Res
Galindo-Murillo, Robertson, Zgarbova, ˇponer, None
Gao, Yan, Huang, Liu, Zhao et al., Structure of the RNA-dependent RNA polymerase from COVID-19 virus, Science
Garcı ´a-Iriepa, Hognon, France ´s-Monerris, Iriepa, Miclot et al., Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-Converting Enzyme 2. Effects of Possible Ligands, J. Phys. Chem. Lett
Gordon, Jang, Bouhaddou, Xu, Obernier et al., A SARS-CoV-2 protein interaction map reveals targets for drug repurposing, Nature
Gray, High-resolution protein-protein docking, Curr. Opin. Struct. Biol
Health, Clinical Trials database
Hegazy, Alghamdi, Shouman, Hegazy, Mass Chemoprophylaxis with Ivermectin against COVID-19 Pandemic: Review and Authors' Perspective, Acta Sci. Med. Sci
Heidary, Gharebaghi, Ivermectin: a systematic review from antiviral effects to COVID-19 complementary regimen, J. Antibiot
Hete, Van Der, Spoel, Efficient docking of peptides to proteins without prior knowledge of the binding site, Protein Sci
Hillen, Kokic, Farnung, Dienemann, Tegunov et al., Structure of replicating SARS-CoV-2 polymerase, Nature
Hognon, Miclot, Iriepa, France ´s-Monerris, Grandemange et al., Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses, J. Phys. Chem. Lett
Hopkins, Le Grand, Walker, Roitberg, Long-time-step molecular dynamics through hydrogen mass repartitioning, J. Chem. Theory Comput
Hornak, Abel, Okur, Strockbine, Roitberg et al., Comparison of multiple Amber force fields and development of improved protein backbone parameters, Proteins: Struct., Funct., Bioinf
Hosseini, Chen, Xiao, Wang, Computational molecular docking and virtual screening revealed promising SARS-CoV-2 drugs, Precis, Clin. Med
Hou, Chiba, Halfmann, Ehre, Kuroda et al., SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo, Science
Hsu, Kuo, Chang, Chang, Chou et al., Mechanism of the maturation process of SARS-CoV 3CL protease, J. Biol. Chem
Huang, Chen, Shaffer, Crystal structures of human GlyRa3 bound to ivermectin, Structure
Humphrey, Dalke, Schulten, VMD: Visual molecular dynamics, J. Mol. Graphics
Huynh, Wang, Luan, Silico Exploration of Molecular Mechanism of Clinically Oriented Drugs for Possibly Inhibiting SARS-CoV-2's Main Protease, J. Phys. Chem. Lett
Islam, Parves, Paul, Uddin, Rahman et al., A Molecular Modeling Approach to Identify Effective Antiviral Phytochemicals against the Main Protease of SARS-CoV-2, J. Biomol. Struct. Dyn
Ivani, Dans, Noy, Pe ´rez, Faustino et al., PARMBSC1: A refined force-field for DNA simulations, Nat. Methods
Jin, Du, Xu, Deng, Liu et al., Structure of Mpro from COVID-19 virus and discovery of its inhibitors, Nature
Jin, Feng, Rong, Pan, Inaba et al., The antiparasitic drug ivermectin is a novel FXR ligand that regulates metabolism, Nat. Commun
Jo, Kim, Shin, Kim, Inhibition of SARS-CoV 3CL protease by flavonoids, J. Enzyme Inhib. Med. Chem
Jorgensen, Chandrasekhar, Madura, Impey, Klein, Comparison of simple potential functions for simulating liquid water, J. Chem. Phys
Khan, Ali, Wang, Irfan, Khan et al., Marine natural compounds as potents inhibitors against the main protease of SARS-CoV-2. A molecular dynamic study, J. Biomol. Struct. Dyn
Khan, Khan, Debnath, Nath, Al Mahtab et al., Ivermectin Treatment May Improve the Prognosis of Patients With COVID-19, Arch. Bronconeumol
Krolewiecki, Lifschitz, Moragas, Travacio, Valentini et al., Antiviral effect of high-dose ivermectin in adults with COVID-19: A proof-of-concept randomized trial, EClinicalMedicine
Kusov, Tan, Alvarez, Enjuanes, Hilgenfeld, A G-quadruplex-binding macrodomain within the ''SARSunique domain'' is essential for the activity of the SARS-coronavirus replication-transcription complex, Virology
Lai, Hanchapola, Steer, Smith, Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: Determinants and constraints, Biochemistry
Lan, Ge, Yu, Shan, Zhou et al., Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor, Nature
Lehrer, Rheinstein, Ivermectin Docks to the SARS-CoV-2 Spike Receptor-binding Domain Attached to ACE2, Vivo
Lei, Kusov, Hilgenfeld, Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein, Antiviral Res
Lesk, Chothia, How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins, J. Mol. Biol
Li, Miao, Li, Zhang, Kainov et al., Ivermectin effectively inhibits hepatitis E virus replication, requiring the host nuclear transport protein importin a1, Arch. Virol
Macchiagodena, Pagliai, Andreini, Rosato, Procacci, Upgrading and Validation of the AMBER Force Field for Histidine and Cysteine Zinc(II)-Binding Residues in Sites with Four Protein Ligands, J. Chem. Inf. Model
Macchiagodena, Pagliai, Procacci, Identification of potential binders of the main protease 3CLpro of the COVID-19 via structure-based ligand design and molecular modeling, Chem. Phys. Lett
Mahanta, Chowdhury, Gogoi, Goswami, Borah et al., Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV-2: an in silico based approach, J. Biomol. Struct. Dyn
Mahmud, Rahman, Alam, Ahmed, Kabir et al., Ivermectin in combination with doxycycline for treating COVID-19 symptoms: a randomized trial, J. Int. Med. Res
Maier, Martinez, Kasavajhala, Wickstrom, Hauser et al., ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB, J. Chem. Theory Comput
Martyna, Tobias, Klein, Constant pressure molecular dynamics algorithms, J. Chem. Phys
Maurya, A Combination of Ivermectin and Doxycycline Possibly Blocks the Viral Entry and Modulate the Innate Immune Response in COVID-19 Patients, doi:10.26434/chemrxiv.12630539.v1
Mercurio, Tragni, Busto, De Grassi, Pierri, Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies, Cell. Mol. Life Sci
Mody, Ho, Wills, Mawri, Lawson et al., Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents, Commun. Biol
Moeller, Shi, Demir, Banerjee, Yin et al., Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN
Moliner, Revealing the molecular mechanisms of proteolysis of SARS-CoV-2 Mpro by QM/ MM computational methods, Chem. Sci
Morris, Huey, Lindstrom, Sanner, Belew et al., AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility, J. Comput. Chem
Mudatsir, Yufika, Nainu, Frediansyah, Megawati et al., Antiviral Activity of Ivermectin Against SARS-CoV-2: An Old-Fashioned Dog with a New Trick-A Literature Review, Sci. Pharm
Muramatsu, Takemoto, Kim, Wang, Nishii et al., SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity, Proc. Natl. Acad. Sci. U. S. A
Olliaro, What does 95% COVID-19 vaccine efficacy really mean?, Lancet Infect. Dis
Otyepka, Jurec, Cheatham, Assessing the Current State of Amber Force Field Modifications for DNA, J. Chem. Theory Comput
Pen ˜a-Silva, Duffull, Steer, Jaramillo-Rincon, Gwee et al., Pharmacokinetic considerations on the repurposing of ivermectin for treatment of COVID-19, Br, J. Clin. Pharmacol
Phillips, Braun, Wang, Gumbart, Tajkhorshid et al., Scalable molecular dynamics with NAMD, J. Comput. Chem
Prabakaran, Xiao, Dimitrov, A model of the ACE2 structure and function as a SARS-CoV receptor, Biochem. Biophys. Res. Commun
Ramajayam, Tan, Liang, Recent development of 3C and 3CL protease inhibitors for anticoronavirus and anti-picornavirus drug discovery, Biochem. Soc. Trans
Ramos-Guzma ´n, Ruiz-Pernı ´a, Tun ˜o ´n, A microscopic description of SARS-CoV-2 main protease inhibition with Michael acceptors. Strategies for improving inhibitor design, Chem. Sci
Ramos-Guzma ´n, Ruiz-Pernı ´a, Tun ˜o ´n, Multiscale simulations of SARS-CoV-2 3CL protease inhibition with aldehyde derivatives. Role of protein and inhibitor conformational changes in the reaction mechanism, ACS Catal
Ramos-Guzma ´n, Ruiz-Pernı ´a, Tun ˜o ´n, Ruiz-Pernı ´a, Tun ˜o ´n, Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale DFT/MM Methods, ACS Catal
Ratia, Kilianski, Baez-Santos, Baker, Mesecar, Structural basis for the ubiquitin-linkage specificity and deISGylating activity of SARS-CoV papain-like protease, PLoS Pathog
Ratia, Pegan, Takayama, Sleeman, Coughlin et al., A noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication, Proc. Natl. Acad. Sci. U. S. A
Roe, Cheatham, PTRAJ and CPPTRAJ: Software for Processing and Analysis of Molecular Dynamics Trajectory Data, J. Chem. Theory Comput
Saha, Raihan, The binding mechanism of ivermectin and levosalbutamol with spike protein of SARS-CoV-2, Struct. Chem
Shang, Wan, Luo, Ye, Geng et al., Cell entry mechanisms of SARS-CoV-2, Proc. Natl. Acad. Sci. U. S. A
Shang, Ye, Shi, Wan, Luo et al., Structural basis of receptor recognition by SARS-CoV-2, Nature
Sharma, Bhardwaj, Singh, Rajendran, Purohit et al., An in-silico evaluation of different bioactive molecules of tea for their inhibition potency against non structural protein-15 of SARS-CoV-2, Food Chem
Sharun, Dhama, Patel, Pathak, Tiwari et al., Ivermectin, a new candidate therapeutic against SARS-CoV-2/COVID-19, Ann. Clin. Microbiol. Antimicrob
Shin, Mukherjee, Grewe, Bojkova, Baek et al., Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity, Nature
Shoemark, Colenso, Toelzer, Gupta, Sessions et al., Molecular Simulations suggest Vitamins, Retinoids and Steroids as Ligands of the Free Fatty Acid Pocket of the SARS-CoV-2 Spike Protein, Angew. Chem., Int. Ed
Singh, Bhardwaj, Das, Purohit, A computational approach for rational discovery of inhibitors for non-structural protein 1 of SARS-CoV-2, Comput. Biol. Med
Singh, Bhardwaj, Sharma, Purohit, Kumar, In-silico evaluation of bioactive compounds from tea as potential SARS-CoV-2 nonstructural protein 16 inhibitors, J. Tradit. Complement. Med, doi:10.1016/j.jtcme.2021.05.005
Sk, Roy, Jonniya, Poddar, Kar, Elucidating biophysical basis of binding of inhibitors to SARS-CoV-2 main protease by using molecular dynamics simulations and free energy calculations, J. Biomol. Struct. Dyn
Sztain, Amaro, Mccammon, Elucidation of Cryptic and Allosteric Pockets within the SARS-CoV-2 Main Protease, J. Chem. Inf. Model
Tan, Vonrhein, Smart, Bricogne, Bollati et al., The SARS-Unique Domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes, PLoS Pathog
Trisolini, Gambacorta, Gorgoglione, Montaruli, Laera et al., FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function, J. Clin. Med
Trott, Olson, AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading, J. Comput. Chem
Tu, Chien, Yarmishyn, Lin, Luo et al., A Review of SARS-CoV-2 and the Ongoing Clinical Trials, Int. J. Mol. Sci
Turon ˇova, Sikora, Schu ¨rmann, Hagen, Welsch et al., In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges, Science
Wang, Cieplak, Kollman, How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?, J. Comput. Chem
Wang, Wolf, Caldwell, Kollman, Case, Development and testing of a general amber force field, J. Comput. Chem
Wang, Zhang, Wu, Niu, Song et al., Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2, Cell
Watkins, Preventing a covid-19 pandemic, BMJ
Xie, Liu, Liu, Zhang, Zou et al., Neutralization of SARS-CoV-2 spike 69/70 deletion, E484K and N501Y variants by BNT162b2 vaccine-elicited sera, Nat. Med
Yan, Xu, Zou, Fully blind docking at the atomic level for protein-peptide complex structure prediction, Structure
Yan, Zhang, Li, Xia, Guo et al., Structural basis for the recognition of SARS-CoV-2 by fulllength human ACE2, Science
Yang, Atkinson, Wang, Lee, Bogoyevitch et al., The broad spectrum antiviral ivermectin targets the host nuclear transport importin a/b1 heterodimer, Antiviral Res
Yang, Yang, Ding, Liu, Lou et al., The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor, Proc. Natl. Acad. Sci. U. S. A
Yuriev, Holien, Ramsland, Improvements, trends, and new ideas in molecular docking: 2012-2013 in review, J. Mol. Recognit
Zgarbova, ˇponer, Otyepka, Cheatham, Galindo-Murillo et al., Refinement of the Sugar-Phosphate Backbone Torsion Beta for AMBER Force Fields Improves the Description of Z-and B-DNA, J. Chem. Theory Comput
Zhang, Lin, Sun, Curth, Drosten et al., Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved a-ketoamide inhibitors, Science
Zhou, Hou, Shen, Huang, Martin et al., Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2, Cell Discovery
Zhou, Yang, Wang, Hu, Zhang et al., A pneumonia outbreak associated with a new coronavirus of probable bat origin, Nature
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