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Nikhil Prasad  Fact checked by:Thailand Medical News Team Jan 17, 2025  15 hours, 23 minutes ago

Scientists in China Discover That Glycyrrhetinic Acid Targets SARS-CoV-2 Fusion Peptides

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Scientists in China Discover That Glycyrrhetinic Acid Targets SARS-CoV-2 Fusion Peptides
Nikhil Prasad  Fact checked by:Thailand Medical News Team Jan 17, 2025  15 hours, 23 minutes ago
Medical News: The SARS-CoV-2 virus, responsible for the global COVID-19 pandemic, primarily invades human cells by utilizing its spike protein to bind to the ACE2 receptors on cell membranes. A specific region of the spike protein, called the fusion peptide (FP), plays a crucial role in this process. Located between residues 815-828, the FP sequence is conserved across coronaviruses and is vital for facilitating the virus's membrane fusion with host cells.


Scientists in China Discover That Glycyrrhetinic Acid Targets SARS-CoV-2 Fusion Peptides

Recent research conducted by scientists from Jiangsu University and Yixing Hospital affiliated with Jiangsu University sheds light on potential strategies to inhibit the FP. This Medical News report delves into how certain drug molecules could prevent the SARS-CoV-2 FP from binding to cell membranes, thereby thwarting the virus’s ability to infect cells.
 
The Study Approach and Objectives
The study explored three drug molecules - Neferine (Nef), Glycyrrhetinic Acid (GA), and Quercetin (Qct) - for their effectiveness in inhibiting the FP's membrane fusion process. These compounds were selected based on prior evidence of their antiviral properties. By combining molecular dynamics (MD) simulations and experimental methods, researchers aimed to determine which molecule exhibited the most robust inhibitory effects.
 
The study began with MD simulations to observe how each drug interacted with the FP sequence. Researchers then conducted cellular experiments to validate their computational findings.
 
Key Findings of the Study
-Glycyrrhetinic Acid Shows Superior Inhibition
Among the three molecules tested, Glycyrrhetinic Acid demonstrated the strongest binding affinity to the FP.
 
Glycyrrhetinic acid is a pentacyclic triterpenoid found in licorice. It is also the main metabolite of glycyrrhizin
 
The MD simulations revealed that GA formed stable interactions with critical FP residues, particularly L821, L822, F823, and L828. These interactions disrupted the FP's ability to fuse with the cell membrane. In contrast, Neferine and Quercetin exhibited weaker binding affinities and were less effective at inhibiting the fusion process.
 
-Experimental Validation
To confirm the computational results, researchers performed FITC fluorescence staining experiments. The FP was conjugated with a fluorescent marker and introduced to mouse fibroblast cells (L929) to observe its interaction with cell membranes. When treated with Glycyrrhetinic Acid, a significant reduction in fluorescence intensity was observed. This finding indicated that GA successfully interfered with the FP's binding ability and disrupted its localization on the cell membrane.
 
-Insights Into Mechanism
Further analysis showed that GA’s inhibitory effect was primarily due to va n der Waals (vdW) forces acting on hydrophobic residues within the FP sequence. Additionally, the study highlighted that GA altered the hydrophobicity and amphiphilic balance of the FP, making it less capable of interacting with the cell membrane.
 
Broader Implications
The findings provide valuable insights into how FP-targeted drugs can prevent the fusion of SARS-CoV-2 with host cells. By targeting specific residues on the FP, GA effectively inhibited the virus's entry mechanism. This approach offers a promising avenue for antiviral drug development, especially as the FP is highly conserved across coronaviruses, making it a universal target.
 
Conclusions and Future Directions
The study highlights the potential of Glycyrrhetinic Acid as a therapeutic candidate against SARS-CoV-2. By interfering with the FP's ability to bind to cell membranes, GA could significantly reduce the virus’s infectivity. The researchers suggest that further exploration of FP-targeted drugs could lead to the development of new antiviral therapies not only for SARS-CoV-2 but also for other viruses with similar entry mechanisms.
 
These findings underscore the importance of understanding molecular interactions at the viral entry level. By focusing on highly conserved sequences like the FP, researchers can develop drugs that are effective across a range of viral strains and mutations. Future studies should focus on optimizing the molecular structure of GA to enhance its efficacy and exploring its potential in clinical settings.
 
The study findings were published in the peer-reviewed journal: CHEMNANOMAT
https://aces.onlinelibrary.wiley.com/doi/10.1002/cnma.202400614
 
For the latest COVID-19 News, keep on logging to Thailand Medical News.
 
Read Also:
https://www.thailandmedical.news/news/russian-scientist-uncover-how-sars-cov-2-fusion-peptides-disrupt-host-cell-membranes
 
https://www.thailandmedical.news/news/fusion-peptide-of-sars-cov-2-unveiled-as-a-key-agent-in-membrane-disruption
 
https://www.thailandmedical.news/news/new-insights-on-covid-19-fusion-peptides-could-lead-to-better-antiviral-treatments
 
https://www.thailandmedical.news/news/sars-cov-2-spike-s-fusion-peptide-binds-to-negatively-charged-phospholipids-in-cell-membranes-of-host
 
https://www.thailandmedical.news/articles/coronavirus
 

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