All Studies Meta Analysis Recent:

Comparative Docking Studies on Curcumin with COVID-19 Proteins

Suravajhala et al., MDPI AG, doi:10.20944/preprints202005.0439.v3

Jun 2020

Post
Facebook

Source PDF All Studies Meta AnalysisMeta

Curcumin for COVID-19

15th treatment shown to reduce risk in February 2021

^*, now with p = 0.0000000096 from 27 studies.

Lower risk for mortality, ventilation, hospitalization, progression, recovery, and viral clearance.

No treatment is 100% effective. Protocols combine treatments. ^* >10% efficacy, ≥3 studies.

4,500+ studies for 81 treatments. c19early.org

In Silico study showing high binding affinity for the SARS-CoV-2 nucleocapsid and nsp10 proteins with curcumin. Authors propose curcumin for COVID-19 drug development.

45 preclinical studies support the efficacy of curcumin for COVID-19:

24 In Silico studies1-24

20 In Vitro studies1,5,7,11,17,21,25-38

1 In Vivo animal study5

In Silico studies predict inhibition of SARS-CoV-2 with curcumin or metabolites via binding to the spikeA,5,10,12,18,21 (and specifically the receptor binding domainB,8,11,14), M^proC,5,7,9-11,13,14,16,19,21,22,24,35, RNA-dependent RNA polymeraseD,11,20, ACE2E,12,13,15, nucleocapsidF,6,23, nsp10G,23, and helicaseH,25 proteins. In Vitro studies demonstrate inhibition of the spikeA,30 (and specifically the receptor binding domainB,38), M^proC,17,30,35,37, ACE2E,38, and TMPRSS2I,38 proteins. In Vitro studies demonstrate efficacy in Calu-3J,36, A549K,30, 293TL,1, HEK293-hACE2M,17,28, 293T/hACE2/TMPRSS2N,29, Vero E6O,7,11,21,28,30-32,34,36, and SH-SY5YP,27 cells. Curcumin is predicted to inhibit the interaction between the SARS-CoV-2 spike protein receptor binding domain and the human ACE2 receptor for the delta and omicron variants8, decreases pro-inflammatory cytokines induced by SARS-CoV-2 in peripheral blood mononuclear cells34, and alleviates SARS-CoV-2 spike protein-induced mitochondrial membrane damage and oxidative stress1.

Important missing comments or errors? Let us know.

Study covers ivermectin and curcumin.

1. Zhang et al., Computational Discovery of Mitochondrial Dysfunction Biomarkers in Severe SARS-CoV-2 Infection: Facilitating Pytomedicine Screening, Phytomedicine, doi:10.1016/j.phymed.2024.155784.sciencedirect.com, doi.org.

2. Öztürkkan et al., In Silico investigation of the effects of curcuminoids on the spike protein of the omicron variant of SARS-CoV-2, Baku State University Journal of Chemistry and Material Sciences, 1:2, bsuj.bsu.edu.az/uploads/pdf/ec4204d62f7802de54e6092bf7860029.pdf.edu.az.

3. Yunze et al., Therapeutic effect and potential mechanism of curcumin, an active ingredient in Tongnao Decoction, on COVID-19 combined with stroke: a network pharmacology study and GEO database mining, Research Square, doi:10.21203/rs.3.rs-4329762/v1.researchsquare.com, doi.org.

4. Agamah et al., Network-based multi-omics-disease-drug associations reveal drug repurposing candidates for COVID-19 disease phases, ScienceOpen, doi:10.58647/DRUGARXIV.PR000010.v1.scienceopen.com, doi.org.

5. Boseila et al., Throat spray formulated with virucidal Pharmaceutical excipients as an effective early prophylactic or treatment strategy against pharyngitis post-exposure to SARS CoV-2, European Journal of Pharmaceutics and Biopharmaceutics, doi:10.1016/j.ejpb.2024.114279.sciencedirect.com, doi.org.

6. Hidayah et al., Bioinformatics study of curcumin, demethoxycurcumin, bisdemethoxycurcumin and cyclocurcumin compounds in Curcuma longa as an antiviral agent via nucleocapsid on SARS-CoV-2 inhibition, International Conference on Organic and Applied Chemistry, doi:10.1063/5.0197724.aip.org, doi.org.

7. Singh et al., Unlocking the potential of phytochemicals in inhibiting SARS-CoV-2 M Pro protein - An in-silico and cell-based approach, Research Square, doi:10.21203/rs.3.rs-3888947/v1.researchsquare.com, doi.org.

8. Kant et al., Structure-based drug discovery to identify SARS-CoV2 spike protein–ACE2 interaction inhibitors, Journal of Biomolecular Structure and Dynamics, doi:10.1080/07391102.2023.2300060.tandfonline.com, doi.org.

9. Naderi Beni et al., In silico studies of anti-oxidative and hot temperament-based phytochemicals as natural inhibitors of SARS-CoV-2 Mpro, PLOS ONE, doi:10.1371/journal.pone.0295014.plos.org, doi.org.

10. Moschovou et al., Exploring the Binding Effects of Natural Products and Antihypertensive Drugs on SARS-CoV-2: An In Silico Investigation of Main Protease and Spike Protein, International Journal of Molecular Sciences, doi:10.3390/ijms242115894.mdpi.com, doi.org.

11. Eleraky et al., Curcumin Transferosome-Loaded Thermosensitive Intranasal in situ Gel as Prospective Antiviral Therapy for SARS-Cov-2, International Journal of Nanomedicine, doi:10.2147/IJN.S423251.dovepress.com, doi.org.

12. Singh (B) et al., Computational studies to analyze effect of curcumin inhibition on coronavirus D614G mutated spike protein, The Seybold Report, doi:10.17605/OSF.IO/TKEXJ.ac.in, doi.org.

13. Thapa et al., In-silico Approach for Predicting the Inhibitory Effect of Home Remedies on Severe Acute Respiratory Syndrome Coronavirus-2, Makara Journal of Science, doi:10.7454/mss.v27i3.1609.ac.id, doi.org.

14. Srivastava et al., Paradigm of Well-Orchestrated Pharmacokinetic Properties of Curcuminoids Relative to Conventional Drugs for the Inactivation of SARS-CoV-2 Receptors: An In Silico Approach, Stresses, doi:10.3390/stresses3030043.mdpi.com, doi.org.

15. Alkafaas et al., A study on the effect of natural products against the transmission of B.1.1.529 Omicron, Virology Journal, doi:10.1186/s12985-023-02160-6.biomedcentral.com, doi.org.

16. Winih Kinasih et al., Analisis in silico interaksi senyawa kurkuminoid terhadap enzim main protease 6LU7 dari SARS-CoV-2, Duta Pharma Journal, doi:10.47701/djp.v3i1.2904.ac.id, doi.org.

17. Wu et al., Potential Mechanism of Curcumin and Resveratrol against SARS-CoV-2, Research Square, doi:10.21203/rs.3.rs-2780614/v1.researchsquare.com, doi.org.

18. Nag et al., Curcumin inhibits spike protein of new SARS-CoV-2 variant of concern (VOC) Omicron, an in silico study, Computers in Biology and Medicine, doi:10.1016/j.compbiomed.2022.105552.sciencedirect.com, doi.org.

19. Rampogu et al., Molecular Docking and Molecular Dynamics Simulations Discover Curcumin Analogue as a Plausible Dual Inhibitor for SARS-CoV-2, International Journal of Molecular Sciences, doi:10.3390/ijms23031771.mdpi.com, doi.org.

20. Singh (C) et al., Potential of turmeric-derived compounds against RNA-dependent RNA polymerase of SARS-CoV-2: An in-silico approach, Computers in Biology and Medicine, doi:10.1016/j.compbiomed.2021.104965.sciencedirect.com, doi.org.

21. Kandeil et al., Bioactive Polyphenolic Compounds Showing Strong Antiviral Activities against Severe Acute Respiratory Syndrome Coronavirus 2, Pathogens, doi:10.3390/pathogens10060758.mdpi.com, doi.org.

22. Rajagopal et al., Activity of phytochemical constituents of Curcuma longa (turmeric) and Andrographis paniculata against coronavirus (COVID-19): an in silico approach, Future Journal of Pharmaceutical Sciences, doi:10.1186/s43094-020-00126-x.springeropen.com, doi.org.

23. Suravajhala et al., Comparative Docking Studies on Curcumin with COVID-19 Proteins, MDPI AG, doi:10.20944/preprints202005.0439.v3.preprints.org, doi.org.

24. Sekiou et al., In-Silico Identification of Potent Inhibitors of COVID-19 Main Protease (Mpro) and Angiotensin Converting Enzyme 2 (ACE2) from Natural Products: Quercetin, Hispidulin, and Cirsimaritin Exhibited Better Potential Inhibition than Hydroxy-Chloroquine Against COVID-19 Main Protease Active Site and ACE2, ChemRxiv, doi:10.26434/chemrxiv.12181404.v1.chemrxiv.org, doi.org.

25. Li et al., Thermal shift assay (TSA)-based drug screening strategy for rapid discovery of inhibitors against the Nsp13 helicase of SARS-CoV-2, Animals and Zoonoses, doi:10.1016/j.azn.2024.06.001.sciencedirect.com, doi.org.

26. Kamble et al., Nanoparticulate curcumin spray imparts prophylactic and therapeutic properties against SARS-CoV-2, Emergent Materials, doi:10.1007/s42247-024-00754-6.springer.com, doi.org.

27. Nicoliche et al., Antiviral, anti-inflammatory and antioxidant effects of curcumin and curcuminoids in SH-SY5Y cells infected by SARS-CoV-2, Scientific Reports, doi:10.1038/s41598-024-61662-7.nature.com, doi.org.

28. Nittayananta et al., A novel film spray containing curcumin inhibits SARS-CoV-2 and influenza virus infection and enhances mucosal immunity, Virology Journal, doi:10.1186/s12985-023-02282-x.biomedcentral.com, doi.org.

29. Septisetyani et al., Curcumin and turmeric extract inhibited SARS-CoV-2 pseudovirus cell entry and Spike mediated cell fusion, bioRxiv, doi:10.1101/2023.09.28.560070.biorxiv.org, doi.org.

30. Mohd Abd Razak et al., In Vitro Anti-SARS-CoV-2 Activities of Curcumin and Selected Phenolic Compounds, Natural Product Communications, doi:10.1177/1934578X231188861.sagepub.com, doi.org.

31. Teshima et al., Antiviral activity of curcumin and its analogs selected by an artificial intelligence-supported activity prediction system in SARS-CoV-2-infected VeroE6 cells, Natural Product Research, doi:10.1080/14786419.2023.2194647.tandfonline.com, doi.org.

32. Leka et al., In vitro antiviral activity against SARS-CoV-2 of common herbal medicinal extracts and their bioactive compounds, Phytotherapy Research, doi:10.1002/ptr.7463.wiley.com, doi.org.

33. Goc et al., Inhibitory effects of specific combination of natural compounds against SARS-CoV-2 and its Alpha, Beta, Gamma, Delta, Kappa, and Mu variants, European Journal of Microbiology and Immunology, doi:10.1556/1886.2021.00022.akjournals.com, doi.org.

34. Marín-Palma et al., Curcumin Inhibits In Vitro SARS-CoV-2 Infection In Vero E6 Cells through Multiple Antiviral Mechanisms, Molecules, doi:10.3390/molecules26226900.mdpi.com, doi.org.

35. Bahun et al., Inhibition of the SARS-CoV-2 3CLpro main protease by plant polyphenols, Food Chemistry, doi:10.1016/j.foodchem.2021.131594.sciencedirect.com, doi.org.

36. Bormann et al., Turmeric Root and Its Bioactive Ingredient Curcumin Effectively Neutralize SARS-CoV-2 In Vitro, Viruses, doi:10.3390/v13101914.mdpi.com, doi.org.

37. Guijarro-Real et al., Potential In Vitro Inhibition of Selected Plant Extracts against SARS-CoV-2 Chymotripsin-Like Protease (3CLPro) Activity, Foods, doi:10.3390/foods10071503.mdpi.com, doi.org.

38. Goc (B) et al., Phenolic compounds disrupt spike-mediated receptor-binding and entry of SARS-CoV-2 pseudo-virions, PLOS ONE, doi:10.1371/journal.pone.0253489.plos.org, doi.org.

a. The trimeric spike (S) protein is a glycoprotein that mediates viral entry by binding to the host ACE2 receptor, is critical for SARS-CoV-2's ability to infect host cells, and is a target of neutralizing antibodies. Inhibition of the spike protein prevents viral attachment, halting infection at the earliest stage.

b. The receptor binding domain is a specific region of the spike protein that binds ACE2 and is a major target of neutralizing antibodies. Focusing on the precise binding site allows highly specific disruption of viral attachment with reduced potential for off-target effects.

c. The main protease or M^pro, also known as 3CL^pro or nsp5, is a cysteine protease that cleaves viral polyproteins into functional units needed for replication. Inhibiting M^pro disrupts the SARS-CoV-2 lifecycle within the host cell, preventing the creation of new copies.

d. RNA-dependent RNA polymerase (RdRp), also called nsp12, is the core enzyme of the viral replicase-transcriptase complex that copies the positive-sense viral RNA genome into negative-sense templates for progeny RNA synthesis. Inhibiting RdRp blocks viral genome replication and transcription.

e. The angiotensin converting enzyme 2 (ACE2) protein is a host cell transmembrane protein that serves as the cellular receptor for the SARS-CoV-2 spike protein. ACE2 is expressed on many cell types, including epithelial cells in the lungs, and allows the virus to enter and infect host cells. Inhibition may affect ACE2's physiological function in blood pressure control.

f. The nucleocapsid (N) protein binds and encapsulates the viral genome by coating the viral RNA. N enables formation and release of infectious virions and plays additional roles in viral replication and pathogenesis. N is also an immunodominant antigen used in diagnostic assays.

g. Non-structural protein 10 (nsp10) serves as an RNA chaperone and stabilizes conformations of nsp12 and nsp14 in the replicase-transcriptase complex, which synthesizes new viral RNAs. Nsp10 disruption may destabilize replicase-transcriptase complex activity.

h. The helicase, or nsp13, protein unwinds the double-stranded viral RNA, a crucial step in replication and transcription. Inhibition may prevent viral genome replication and the creation of new virus components.

i. Transmembrane protease serine 2 (TMPRSS2) is a host cell protease that primes the spike protein, facilitating cellular entry. TMPRSS2 activity helps enable cleavage of the spike protein required for membrane fusion and virus entry. Inhibition may especially protect respiratory epithelial cells, buy may have physiological effects.

j. Calu-3 is a human lung adenocarcinoma cell line with moderate ACE2 and TMPRSS2 expression and SARS-CoV-2 susceptibility. It provides a model of the human respiratory epithelium, but many not be ideal for modeling early stages of infection due to the moderate expression levels of ACE2 and TMPRSS2.

k. A549 is a human lung carcinoma cell line with low ACE2 expression and SARS-CoV-2 susceptibility. Viral entry/replication can be studied but the cells may not replicate all aspects of lung infection.

l. 293T is a human embryonic kidney cell line that can be engineered for high ACE2 expression and SARS-CoV-2 susceptibility. 293T cells are easily transfected and support high protein expression.

m. HEK293-hACE2 is a human embryonic kidney cell line with high ACE2 expression and SARS-CoV-2 susceptibility. Cells have been transfected with a plasmid to express the human ACE2 (hACE2) protein.

n. 293T/hACE2/TMPRSS2 is a human embryonic kidney cell line engineered for high ACE2 and TMPRSS2 expression, which mimics key aspects of human infection. 293T/hACE2/TMPRSS2 cells are very susceptible to SARS-CoV-2 infection.

o. Vero E6 is an African green monkey kidney cell line with low/no ACE2 expression and high SARS-CoV-2 susceptibility. The cell line is easy to maintain and supports robust viral replication, however the monkey origin may not accurately represent human responses.

p. SH-SY5Y is a human neuroblastoma cell line that exhibits neuronal phenotypes. It is commonly used as an in vitro model for studying neurotoxicity, neurodegenerative diseases, and neuronal differentiation.

Suravajhala et al., 7 Jun 2020, preprint, 8 authors. Contact: giri@genomixbiotech.com (corresponding author), prash@bisr.res.in.

In Silico studies are an important part of preclinical research, however results may be very different in vivo.

This Paper Curcumin All

Comparative Docking Studies on Curcumin with COVID-19 Proteins

Renuka Suravajhala, Abhinav Parashar, Babita Malik, Viswanathan Arun Nagaraj, Govindarajan Padmanaban, P B Kavi Kishor, Rathnagiri Polavarapu, Prashanth Suravajhala

doi:10.20944/preprints202005.0439.v3

Highlights 1. Our findings confirm the role of Q163 aminoacid site for potential tethered site or target which is in agreement with ivermectin, the best possible and known drug. 2. We have employed a rigorous strategy in screening the docking complexes from a majority of hypothetical genes or orphan open reading frames, structural and non-structural proteins. 3. We believe that the findings presented in our paper will appeal to researchers working on COVID-19, particularly those interested to characteristically screen docking complexes.

Author contributions: GP, PBK and RP ideated the project. RS and AP jointly analysed the structures and modelled the docking complexes. PS performeddid the protein interaction analyses. AP and RS wrote the first draft with PS, PBK, BM and RP. GP, PBK, PS, VAN and RP proofread the manuscript. Competing interests: None

References

Balasco, Esposito, De Simone, Vitagliano, Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms, Protein Sci, doi:10.1002/pro.2279

Bosch, Van Der Zee, De Haan, Rottier, The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex, J. Virol, doi:10.1128/jvi.77.16.8801-8811.2003

Bouvet, Lugari, Posthuma, Coronavirus Nsp10, a critical co-factor for activation of multiple replicative enzymes, J Biol Chem, doi:10.1074/jbc.M114.577353

Chen, Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2′-O-methylation by nsp16/nsp10 protein complex, PLOS Pathog, doi:10.1371/journal.ppat.1002294

Chen, Liu, Guo, Emerging coronaviruses: Genome structure, replication, and pathogenesis, Journal of Medical Virology, doi:10.1002/jmv.25681

Delano, The PyMOL Molecular Graphics System; DeLano Scientific

Dende, Meena, Nagarajan, Nagaraj, Panda et al., Nanocurcumin is superior to native curcumin in preventing degenerative changes in Experimental Cerebral Malaria, Scientific reports, doi:10.1038/s41598-017-10672-9

Dolati, Ahmadi, Aghebti-Maleki, Nanocurcumin is a potential novel therapy for multiple sclerosis by influencing inflammatory mediators, Pharmacol Rep, doi:10.1016/j.pharep.2018.05.008

Hesari, Ghasemi, Salarinia, Biglari, Tabar Molla Hassan et al., Effects of curcumin on NF-κB, AP-1, and Wnt/β-catenin signaling pathway in hepatitis B virus infection, Journal of cellular biochemistry, doi:10.1002/jcb.26829

Hilgenfeld, Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites, Acta Pharm. Sin. B, doi:10.1111/febs.12936Kang

Hoffmann, Kleine-Weber, Schroeder, Krüger, Herrler et al., SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor, Cell, doi:10.1016/j.cell.2020.02.052

Kang, Yang, Hong, Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

Mcbride, Van Zyl, Fielding, The coronavirus nucleocapsid is a multifunctional protein, Viruses, doi:10.3390/v6082991

Morris, AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility, J. Comput. Chem, doi:10.1002/jcc.21256

N M O'boyle, Banck, James, Morley, Vandermeersch et al., Open Babel: An open chemical toolbox, J. Cheminf, doi:10.1186/1758-2946-3-33

Nelson, Dahlin, Bisson, Graham, Pauli et al., The essential medicinal chemistry of curcumin: miniperspective, Journal of medicinal chemistry, doi:10.1021/acs.jmedchem.6b00975

Padmanaban, Nagaraj, Curcumin from turmeric as an adjunct drug?, Chem, doi:10.1016/B978-0-444-64057-4.00006-5

Padmanaban, Nagaraj, Curcumin may defy medicinal chemists, ACS Med. Chem. Lett, doi:10.1021/acsmedchemlett.7b00051

Pettersen, Goddard, Huang, Couch, Greenblatt et al., UCSF Chimera -A Visualization System for Exploratory Research and Analysis, J. Comput. Chem

Prasad, Tyagi, Aggarwal, Recent developments in delivery, bioavailability, absorption and metabolism of curcumin: the golden pigment from golden spice, Cancer Res. Treat. Off. J. Korean Cancer Assoc, doi:10.4143/crt.2014.46.1.2

Rossi, Sanga, Barton, Potential harmful effects of discontinuing ACE-inhibitors and ARBs in COVID-19 patients, Elife, doi:10.7554/eLife.57278

Sampangi-Ramaiah, Vishwakarma, Shaanker, Molecular docking analysis of selected natural products from plants for inhibition of SARS-CoV-2 main protease, Current Science

Soleimani, Sahebkar, Hosseinzadeh, Turmeric (Curcuma longa) and its major constituent (Curcumin) as nontoxic and safe substances: Review, Phytother. Res, doi:10.1002/ptr.6054

Su, Lou, Sun, Zhai, Yang et al., Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10, Journal of Virology, doi:10.1128/JVI.00483-06

Vathsala, Dende, Nagaraj, Bhattacharya, Das et al., Curcuminarteether combination therapy of Plasmodium berghei-infected mice prevents recrudescence through immunomodulation, PLoS One, doi:10.1371/journal.pone.0029442

Walls, Park, Tortorici, Wall, Mcguire et al., Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein, Cell, doi:10.1016/j.cell.2020.02.058

Walls, Tortorici, Snijder, Xiong, Bosch et al., Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion, Proceedings of the National Academy of Sciences, doi:10.1073/pnas.1708727114

Xia, Ye, Shi, Zhou, Hua, Curcumin improves diabetes mellitus-associated cerebral infarction by increasing the expression of GLUT1 and GLUT3, Molecular medicine reports, doi:10.3892/mmr.2017.8085

Yang, Lee, Si, Lee, You et al., Curcumin shows antiviral properties against norovirus, Molecules, doi:10.3390/molecules21101401

Zhou, Liu, Wang, Liu, Li et al., The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha, Journal of Virology, doi:10.1128/JVI.00133-08

{ 'indexed': {'date-parts': [[2023, 2, 5]], 'date-time': '2023-02-05T05:24:08Z', 'timestamp': 1675574648871}, 'posted': {'date-parts': [[2020, 6, 7]]}, 'group-title': 'LIFE SCIENCES', 'reference-count': 0, 'publisher': 'MDPI AG', 'license': [ { 'start': { 'date-parts': [[2020, 6, 7]], 'date-time': '2020-06-07T00:00:00Z', 'timestamp': 1591488000000}, 'content-version': 'unspecified', 'delay-in-days': 0, 'URL': 'http://creativecommons.org/licenses/by/4.0'}], 'content-domain': {'domain': [], 'crossmark-restriction': False}, 'accepted': {'date-parts': [[2020, 6, 5]]}, 'abstract': 'Corona virus disease 2019 (COVID-19) is caused by a Severe Acute Respiratory ' 'Syndrome-Coronavirus 2 (SARS-CoV-2), which is a positive strand RNA virus. The SARS-CoV-2 ' 'genome and its association to SAR-CoV-1 vary from ca. 66% to 96% depending on the type of ' 'betacoronavirdeae family members. With several drugs, viz. chloroquine, hydroxychloroquine, ' 'ivermectin, artemisinin, remdesivir, azithromycin considered for clinical trials, there has ' 'been an inherent need to find distinctive antiviral mechanisms of these drugs. Curcumin, a ' 'natural bioactive molecule has been shown to have a therapeutic potential for various ' 'diseases, but its effect on COVID-19 has not been explored. In this study, we show the ' 'binding potential of curcumin targeted to a variety of SARS-CoV-2 proteins, viz. spike ' 'glycoproteins (PDB ID: 6VYB), nucleocapsid phosphoprotein (PDB ID: 6VYO), membrane ' 'glycoprotein (PDB ID: 6M17) along with nsp10 (PDB ID: 6W4H) and RNA dependent RNA polymerase ' '(PDB ID: 6M71) structures. Our results indicate that curcumin has high binding affinity ' 'towards nucleocapsid and nsp 10 proteins with potential antiviral activity.', 'DOI': '10.20944/preprints202005.0439.v3', 'type': 'posted-content', 'created': {'date-parts': [[2020, 6, 8]], 'date-time': '2020-06-08T15:31:31Z', 'timestamp': 1591630291000}, 'source': 'Crossref', 'is-referenced-by-count': 4, 'title': 'Comparative Docking Studies on Curcumin with COVID-19 Proteins', 'prefix': '10.20944', 'author': [ {'given': 'Renuka', 'family': 'Suravajhala', 'sequence': 'first', 'affiliation': []}, {'given': 'Abhinav', 'family': 'Parashar', 'sequence': 'additional', 'affiliation': []}, {'given': 'Babita', 'family': 'Malik', 'sequence': 'additional', 'affiliation': []}, {'given': 'Viswanathan Arun', 'family': 'Nagaraj', 'sequence': 'additional', 'affiliation': []}, {'given': 'Govindarajan', 'family': 'Padmanaban', 'sequence': 'additional', 'affiliation': []}, {'given': 'PB', 'family': 'Kavi Kishor', 'sequence': 'additional', 'affiliation': []}, {'given': 'Rathnagiri', 'family': 'Polavarapu', 'sequence': 'additional', 'affiliation': []}, { 'ORCID': 'http://orcid.org/0000-0002-8535-278X', 'authenticated-orcid': False, 'given': 'Prashanth', 'family': 'Suravajhala', 'sequence': 'additional', 'affiliation': []}], 'member': '1968', 'container-title': [], 'original-title': [], 'deposited': { 'date-parts': [[2020, 6, 8]], 'date-time': '2020-06-08T15:44:10Z', 'timestamp': 1591631050000}, 'score': 1, 'resource': {'primary': {'URL': 'https://www.preprints.org/manuscript/202005.0439/v3'}}, 'subtitle': [], 'short-title': [], 'issued': {'date-parts': [[2020, 6, 7]]}, 'references-count': 0, 'URL': 'http://dx.doi.org/10.20944/preprints202005.0439.v3', 'relation': { 'is-version-of': [ { 'id-type': 'doi', 'id': '10.20944/preprints202005.0439.v1', 'asserted-by': 'subject'}, { 'id-type': 'doi', 'id': '10.20944/preprints202005.0439.v2', 'asserted-by': 'subject'}], 'has-version': [ { 'id-type': 'doi', 'id': '10.20944/preprints202005.0439.v1', 'asserted-by': 'object'}, { 'id-type': 'doi', 'id': '10.20944/preprints202005.0439.v2', 'asserted-by': 'object'}]}, 'published': {'date-parts': [[2020, 6, 7]]}, 'subtype': 'preprint'}

Download Image

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.

Submit

Post

@CovidAnalysis

FAQ

Public domain CC0 1.0