VSV-G inhibitors constitute a distinctive class of chemical compounds that primarily target the vesicular stomatitis virus glycoprotein (VSV-G) and modulate its biological activity. The VSV-G glycoprotein is an integral component of the vesicular stomatitis virus, a member of the Rhabdoviridae family, which encompasses a broad range of enveloped viruses. The viral glycoprotein plays a pivotal role in mediating viral entry into host cells by facilitating the fusion of the viral envelope with the host cell membrane. VSV-G inhibitors are designed to interfere with this crucial process, thereby impeding the virus's ability to initiate infection and propagate within the host. Structurally, VSV-G inhibitors exhibit remarkable diversity, as they can be synthesized as small organic molecules or even be found innatural sources. Their mechanism of action involves interaction with specific regions of the VSV-G glycoprotein, which may hinder its proper folding, oligomerization, or engagement with cellular receptors. Consequently, the inhibitors disrupt the fusion process between the viral envelope and the host cell membrane, impeding the internalization of the viral genetic material into the host cell and subsequently curbing the progression of viral infection. The development of VSV-G inhibitors is a result of extensive research into the molecular interactions between the virus and its target cells. This class of compounds showcases the intricate nature of the interplay between viral components and host cell machinery, highlighting the ability for novel strategies to counteract viral infections.
In conclusion, VSV-G inhibitors constitute a distinctive class of chemical entities that intricately disrupt the vesicular stomatitis virus glycoprotein's function, impeding the virus's entry into host cells. These compounds represent the culmination of research into the molecular mechanisms of viral infection and hold promise as tools for understanding viral entry processes at a fundamental level. The diversity of their structural composition underscores the intricate nature of the virus-host interaction and presents avenues for the development of antiviral strategies.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $30.00 $52.00 $122.00 $367.00 | 25 | |
Inhibits protein transport between ER and Golgi by disrupting COPI | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $152.00 $515.00 | ||
Disrupts intracellular trafficking by altering ion gradients | ||||||
Methyl-β-cyclodextrin | 128446-36-6 | sc-215379A sc-215379 sc-215379C sc-215379B | 100 mg 1 g 10 g 5 g | $25.00 $65.00 $170.00 $110.00 | 19 | |
Sequesters cholesterol, affecting lipid rafts and membrane fusion | ||||||
Chlorpromazine | 50-53-3 | sc-357313 sc-357313A | 5 g 25 g | $60.00 $108.00 | 21 | |
Alters membrane fluidity and inhibits endocytosis | ||||||
1-Adamantylamine | 768-94-5 | sc-251475 sc-251475A | 1 g 25 g | $38.00 $144.00 | ||
Interferes with viral uncoating and membrane fusion | ||||||
Arbidol Hydrochloride | 131707-23-8 | sc-210834 | 10 mg | $204.00 | ||
Blocks viral entry by interacting with viral envelope protein | ||||||
Nitazoxanide | 55981-09-4 | sc-212397 | 10 mg | $122.00 | 1 | |
Inhibits viral replication and potentially entry | ||||||
Nelfinavir | 159989-64-7 | sc-507314 | 10 mg | $168.00 | ||
Inhibits protease activity involved in viral replication | ||||||
Lovastatin | 75330-75-5 | sc-200850 sc-200850A sc-200850B | 5 mg 25 mg 100 mg | $28.00 $88.00 $332.00 | 12 | |
Inhibits cholesterol synthesis, affecting lipid rafts | ||||||
Toremifene | 89778-26-7 | sc-205868 sc-205868A | 500 mg 1 g | $85.00 $129.00 | 1 | |
Blocks viral entry by affecting fusion of viral envelope with host cell membrane | ||||||