PR inhibitors were the first successful “designer” antiviral drugs. PR inhibitors were developed based upon a clear understanding of the molecular structure and catalytic activity of PR. They are competitive inhibitors of HIV-1 PR and function by inserting into the substrate-binding cleft of PR. The first PR inhibitors were derivatives of small peptides. There are eight approved PR inhibitors and in the presence of these drugs, noninfectious virions are produced from cells containing integrated copies of the HIV genome. PR inhibitors are extremely effective when used in combination NRTIs, perhaps because they target a different step in the virus replication cycle.
https://www.sciencedirect.com/topics/neuroscience/protease-inhibitors
Currently, there are five HIV protease inhibitors approved by FDA for the treatment of HIV infection. These medications work at the final stage of viral replication and attempt to prevent HIV from making new copies of itself by interfering with the HIV protease enzyme. As a result, the new copies of HIV are not able to infect new cells.1 The United States Food and Drug Administration (FDA) approved the new drugs in December, 1995 for Invirase; and March, 1996 for Norvir and Crixivan.
https://www.theinventors.org/library/inventors/bl_protease_inhibitors.htm
Pfizer’s new COVID-19 protease inhibitor drug is not just “repackaged ivermectin”
Pfizer recently announced that its new protease inhibitor-based drug was 89% effective in preventing hospitalization due to COVID-19 and it is seeking an emergency use authorization for it from the FDA. Antivaxxers claim that ivermectin targets the same protease and is being “suppressed” to protect Pfizer’s profits from the new drug. What’s the real story? Hint: Antivaxxers took a grain of truth and—shall we say?—exaggerated. A lot.
Ivermectin
The mechanisms of action of Ivermectin against SARS-CoV-2: An evidence-based clinical review article
Considering the urgency of the ongoing COVID-19 pandemic, detection of various new mutant strains and future potential re-emergence of novel coronaviruses, repurposing of approved drugs such as Ivermectin could be worthy of attention. This evidence-based review article aims to discuss the mechanism of action of ivermectin against SARS-CoV-2 and summarizing the available literature over the years. A schematic of the key cellular and biomolecular interactions between Ivermectin, host cell, and SARS-CoV-2 in COVID-19 pathogenesis and prevention of complications have been proposed.
There is evidence supporting the use of Ivermectin in decreasing mortality figures in patients with SARS-CoV-2 infection.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8203399/
Direct action of Ivermectin on SARS-CoV-2
Level 1: Action on SARS-CoV-2 cell entry
A study by Lehrer S et al observed that Ivermectin docked in the region of leucine 91 of the SARS-CoV-2 spike protein and histidine 378 of the host cell ACE-2 receptor blocking its entry into the host cell [22]. In yet another study by Eweas et al., potential repurposed drugs such as Ivermectin, chloroquine, hydroxychloroquine, remdesivir, and favipiravir were screened and molecular docking with different SARS-CoV-2 target proteins including S and M proteins, RNA-dependent RNA polymerase (RdRp), nucleoproteins, viral proteases, and nsp14, was performed. Ivermectin showed the following 5 important docking properties [23]:
Highest binding affinity to the predicted active site of the S glycoprotein (Mol Dock score −140.584) and protein–ligand interactions (MolDock score−139.371).
Considerable binding affinity to the predicted active site of the SARS-CoV-2 RdRp protein (MolDock score −149.9900) and protein–ligand interactions (MolDock score −147.608), it formed H-bonds with only two amino acids: Cys622 and Asp760.
Highest binding affinity (MolDock score −212.265) to the predicted active site of nsp14.
The highest binding affinity to the active site of the TMPRSS2 protein (MolDock score −174.971) and protein–ligand interactions (MolDock score −180.548). Moreover, it formed five H-bonds with Cys297, Glu299, Gln438, Gly462, and Gly464 amino acid residues present at the predicted active site of the TMPRSS protein
The free binding energy of the spike protein (open) was higher in Ivermectin (−398.536 kJ/mol) than remdesivir (−232.973 kJ/mol).
Fuck the vaccine and fuck Bill Gates
