Analgesics
Antiandrogens
Antihistamines
Azvudine
Bromhexine
Budesonide
Colchicine
Conv. Plasma
Curcumin
Famotidine
Favipiravir
Fluvoxamine
Hydroxychlor..
Ivermectin
Lifestyle
Melatonin
Metformin
Minerals
Molnupiravir
Monoclonals
Naso/orophar..
Nigella Sativa
Nitazoxanide
PPIs
Paxlovid
Quercetin
Remdesivir
Thermotherapy
Vitamins
More

Other
Feedback
Home
 
Top
..
c19early.org COVID-19 treatment researchSelect treatment..Select..
Melatonin Meta
Metformin Meta
Antihistamines Meta
Azvudine Meta Molnupiravir Meta
Bromhexine Meta
Budesonide Meta
Colchicine Meta Nigella Sativa Meta
Conv. Plasma Meta Nitazoxanide Meta
Curcumin Meta PPIs Meta
Famotidine Meta Paxlovid Meta
Favipiravir Meta Quercetin Meta
Fluvoxamine Meta Remdesivir Meta
Hydroxychlor.. Meta Thermotherapy Meta
Ivermectin Meta

Polydatin for COVID-19

Polydatin has been reported as potentially beneficial for treatment of COVID-19. We have not reviewed these studies. See all other treatments.
Hussein et al., In silico drug repurposing using molecular docking and dynamics to target the protein interaction between the SARS-CoV-2 S-glycoprotein and the ACE2 receptor, F1000Research, doi:10.12688/f1000research.131508.2
<ns4:p><ns4:bold>Background:</ns4:bold> The protein interaction between the viral surface S-glycoprotein and the host angiotensin converting enzyme-2 receptor (ACE2) is key to the virulent nature of SARS-CoV-2. The potential role that effective drug repurposing strategies may have to help stem the impact of future outbreaks has been brought to light in the recent COVID-19 pandemic. This study outlines a comprehensive approach towards <ns4:italic>in-silico</ns4:italic> drug discovery which aims to identify hit agents that can be suitably translated into a clinical setting. <ns4:bold>Methods:</ns4:bold> We use two different computational platforms to analyze the viral S-glycoprotein in its bound conformational state to the ACE2 receptor. We employed a comprehensive screening approach to shortlist compounds capable of binding to the viral target interface and corroborated these findings using both Schrödinger’s Glide and AutoDock Vina. Molecular dynamic simulation studies further verified the stability of the interaction at the viral-host protein interface. <ns4:bold>Results:</ns4:bold> Lymecycline, pentagalloylglucose, polydatin, and hexoprenaline were identified as prime candidates for further studies given the robust and stable nature of their interaction at the viral-host interface and relevance for clinical testing. These agents were shown in a 100-nanosecond simulation trajectory to favorably disrupt key binding interactions at the viral-host interface and may potentially inhibit viral entry into host cells. In all hit molecules it was observed that inhibiting the interaction with the following key viral binding residues: Lys17, Gly496, Tyr 505, and key host residues: His34, Asp38, Lys353, played a critical role toward the inhibition of the viral-host protein interaction. <ns4:bold>Conclusions:</ns4:bold> Our study is unique in its comprehensive approach to identify agents that can bind to the S-glycoprotein-ACE2 interface using multiple computational platforms. Among the hit compounds shortlisted in this study, both lymecycline and hexoprenaline may be considered as candidates for preliminarily clinical studies to assess their therapeutic potential in the management of COVID-19 infections.</ns4:p>
Günther et al., X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease, Science, doi:10.1126/science.abf7945
A large-scale screen to target SARS-CoV-2 The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome is initially expressed as two large polyproteins. Its main protease, M pro , is essential to yield functional viral proteins, making it a key drug target. Günther et al. used x-ray crystallography to screen more than 5000 compounds that are either approved drugs or drugs in clinical trials. The screen identified 37 compounds that bind to M pro . High-resolution structures showed that most compounds bind at the active site but also revealed two allosteric sites where binding of a drug causes conformational changes that affect the active site. In cell-based assays, seven compounds had antiviral activity without toxicity. The most potent, calpeptin, binds covalently in the active site, whereas the second most potent, pelitinib, binds at an allosteric site. Science , this issue p. 642
Please send us corrections, updates, or comments. c19early involves the extraction of 100,000+ datapoints from thousands of papers. Community updates help ensure high accuracy. Treatments and other interventions are complementary. All practical, effective, and safe means should be used based on risk/benefit analysis. No treatment or intervention is 100% available and effective for all current and future variants. We do not provide medical advice. Before taking any medication, consult a qualified physician who can provide personalized advice and details of risks and benefits based on your medical history and situation. FLCCC and WCH provide treatment protocols.
  or use drag and drop   
Thanks for your feedback! Please search before submitting papers and note that studies are listed under the date they were first available, which may be the date of an earlier preprint.
Submit