ZINC2112958 for COVID-19
c19early.org
COVID-19 Treatment Clinical Evidence
COVID-19 involves the interplay of 400+ viral and host proteins and factors, providing many therapeutic targets.
c19early analyzes 6,000+ studies for 210+ treatments—over 17 million hours of research.
Only three high-profit early treatments are approved in the US.
In reality, many treatments reduce risk,
with 25 low-cost treatments approved across 163 countries.
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Naso/
oropharyngeal treatment Effective Treatment directly to the primary source of initial infection. -
Healthy lifestyles Protective Exercise, sunlight, a healthy diet, and good sleep all reduce risk.
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Immune support Effective Vitamins A, C, D, and zinc show reduced risk, as with other viruses.
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Thermotherapy Effective Methods for increasing internal body temperature, enhancing immune system function.
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Systemic agents Effective Many systemic agents reduce risk, and may be required when infection progresses.
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High-profit systemic agents Conditional Effective, but with greater access and cost barriers.
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Monoclonal antibodies Limited Utility Effective but rarely used—high cost, variant dependence, IV/SC admin.
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Acetaminophen Harmful Increased risk of severe outcomes and mortality.
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Remdesivir Harmful Increased mortality with longer followup. Increased kidney and liver injury, cardiac disorders.
ZINC2112958 may be beneficial for
COVID-19 according to the study below.
COVID-19 involves the interplay of 400+ viral and host proteins and factors providing many therapeutic targets.
Scientists have proposed 11,000+ potential treatments.
c19early.org analyzes
210+ treatments.
We have not reviewed ZINC2112958 in detail.
, Structure-Based Identification of SARS-CoV-2 nsp10-16 Methyltransferase Inhibitors Using Molecular Dynamics Insights, Current Issues in Molecular Biology, doi:10.3390/cimb47030198
SARS-CoV-2 evades immune detection via nsp10-16 methyltransferase-mediated 2′-O-methylation of viral mRNA, making it a key antiviral target. Our study employed structure-based drug discovery—including virtual screening, molecular docking, and molecular dynamics (MD) simulations—to identify potent inhibitors of nsp10-16. We identified seven promising inhibitors (Z1–Z7) targeting the binding site of the SARS-CoV-2 nsp10-16 methyltransferase, with Z2, Z3, Z4, and Z7 exhibiting strong binding affinities. Further, molecular dynamics simulations confirmed that Z2, Z3, and Z7 effectively stabilized the enzyme by reducing conformational fluctuations and maintaining structural compactness, comparable to the native ligand-bound complex. The conformational deviation revealed that Z2, Z6, and Z7 restricted large-scale conformational transitions, reinforcing their stabilizing effect on the enzyme. The binding free energy calculations ranked Z4 (−37.26 kcal/mol), Z7 (−35.37 kcal/mol), and Z6 (−35.22 kcal/mol) as the strongest binders, surpassing the native tubercidin complex (−23.70 kcal/mol). The interactions analysis identified Asp99, Tyr132, and Cys115 as key stabilizing residues, with Z2, Z6, and Z7 forming high-lifetime hydrogen bonds. The drug-likeness analysis highlighted the selected compounds as promising candidates, exhibiting high gastrointestinal absorption, optimal solubility, and minimal CYP450 inhibition. Further experimental validation and lead optimization are needed to develop potent methyltransferase inhibitors with improved pharmacokinetics and antiviral efficacy.