Glycyrrhizinic acid 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.

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.
Immune support Effective Vitamins A, C, D, and zinc show reduced risk, as with other viruses.
Thermotherapy Effective Methods for increasing internal body temperature, enhancing immune system function.
Systemic agents Effective Many systemic agents reduce risk, and may be required when infection progresses.
High-profit systemic agents Conditional Effective, but with greater access and cost barriers.
Monoclonal antibodies Limited Utility Effective but rarely used—high cost, variant dependence, IV/SC admin.
Acetaminophen Harmful Increased risk of severe outcomes and mortality.
Remdesivir Harmful Increased mortality with longer followup. Increased kidney and liver injury, cardiac disorders.

Glycyrrhizinic acid may be beneficial for COVID-19 according to the studies 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 glycyrrhizinic acid in detail.

Studies suggesting benefit with glycyrrhizinic acid

Wan et al., The Emerging Promise of Pentacyclic Triterpenoid Derivatives as Novel Antiviral Agents Against SARS-CoV-2 Variants, Molecules, doi:10.3390/molecules31020325

The continuous emergence of SARS-CoV-2 variants, especially the Omicron strain with its heightened transmissibility, has posed ongoing challenges to the efficacy of existing vaccine and drug regimens. This situation highlights the pressing demand for antiviral drugs employing novel mechanisms of action. Pentacyclic triterpenoids (PTs), a structurally varied group of compounds derived from plants, exhibit both antiviral and anti-inflammatory activities, making them attractive candidates for further therapeutic development. These natural products, along with their saponin derivatives, show broad-spectrum inhibitory effects against multiple SARS-CoV-2 variants (from Alpha to Omicron) via interactions with multiple targets, such as the spike protein, main protease (Mpro), RNA-dependent RNA polymerase (RdRp), and inflammatory signaling pathways. This review consolidates recent findings on PTs and their saponins, emphasizing their influence on the key structural features required for inhibiting viral attachment, membrane fusion, reverse transcription, and protease function. We systematically summarized the structure–activity relationships and their antiviral results of PTs based on different target proteins in existing studies. Furthermore, this work points toward new strategies for designing multi-target PT-based inhibitors with improved efficacy against Omicron and future variants.

Hanai, T., COVID-19, Infection Inhibitors and Medicines, MDPI AG, doi:10.20944/preprints202501.1042.v1

The fast mutation of COVID-19 viruses still confuses us, and the mRNA vaccines do not inhibit the infection and may protect against the heavy disease. The infection mechanism is described with the protein-protein binding stereo structure; therefore, the infection strength of variants has been estimated from the protein-protein (S-RBD binding with ACE-2) interaction energy values calculated using a molecular mechanics program. The binding strength order was Alfa &lt; Lambda &lt; WT &lt; FE.1 &lt; XBB1.5 &lt; EG.5 ≈ BQ.1 ≈ Alpha+E484K ≈ Omicron XBB.1.16 ≈ Epsilon, Iota &lt; EG.5 &lt; Delta plus ≈ Beta, Kappa B.1.621 ≈ KP.3 ≈ Kappa B.1.617.1 ≈ Delta B.1.517.2 &lt; KP.2 &lt; BA.2.86 ≈ JN.1 ≈ HV.1 ≈ BA.1 &lt; BA.2. The mutation from acidic amino acid to basic amino acid strength the binding. The substitute size of amino acids causes the steric hindrance for the binding. The affinity level supports the infection strength. Various proposed infection inhibitors are quantitatively analyzed. TCA acids and natural polyphenols inhibit the binding of S-RBD to ACE-2. The cocktail dose of known medicines may enhance their performance. The inhibiting multiplication may be achieved using glycated compounds that bind glycoproteins and reduce glycoprotein activities.