Exploring the Targets of Novel Corona Virus and Docking-based Screening of Potential Natural Inhibitors to Combat COVID-19.
COVID-19
Docking- based screening.
Natural inhibitors
Non-structural proteins
SARS-CoV-2 potential targets
Structural proteins
Journal
Current topics in medicinal chemistry
ISSN: 1873-4294
Titre abrégé: Curr Top Med Chem
Pays: United Arab Emirates
ID NLM: 101119673
Informations de publication
Date de publication:
2022
2022
Historique:
received:
12
06
2022
revised:
07
09
2022
accepted:
21
09
2022
pubmed:
26
10
2022
medline:
20
1
2023
entrez:
25
10
2022
Statut:
ppublish
Résumé
There is a need to explore natural compounds against COVID-19 due to their multitargeted actions against various targets of nCoV. They act on multiple sites rather than single targets against several diseases. Thus, there is a possibility that natural resources can be repurposed to combat COVID-19. However, the biochemical mechanisms of these inhibitors were not known. To reveal the mode of anti-nCoV action, structure-based docking plays a major role. The present study is an attempt to explore various potential targets of SARS-CoV-2 and the structure-based screening of various potential natural inhibitors to combat the novel coronavirus.
Identifiants
pubmed: 36281864
pii: CTMC-EPUB-127125
doi: 10.2174/1568026623666221020163831
doi:
Substances chimiques
Antiviral Agents
0
Protease Inhibitors
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2410-2434Informations de copyright
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
Références
Zhou P.; Yang X.L.; Wang X.G.; Hu B.; Zhang L.; Zhang W.; Si H.R.; Zhu Y.; Li B.; Huang C.L.; Chen H.D.; Chen J.; Luo Y.; Guo H.; Jiang R.D.; Liu M.Q.; Chen Y.; Shen X.R.; Wang X.; Zheng X.S.; Zhao K.; Chen Q.J.; Deng F.; Liu L.L.; Yan B.; Zhan F.X.; Wang Y.Y.; Xiao G.F.; Shi Z.L.; A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 2020,579(7798),270-273
doi: 10.1038/s41586-020-2012-7
pubmed: 32015507
Yang H.; Bartlam M.; Rao Z.; Drug design targeting the main protease, the Achilles’ heel of coronaviruses. Curr Pharm Des 2006,12(35),4573-4590
doi: 10.2174/138161206779010369
pubmed: 17168763
Belouzard S.; Millet J.K.; Licitra B.N.; Whittaker G.R.; Mechanisms of coronavirus cell entry mediated by the viral spike protein. Viruses 2012,4(6),1011-1033
doi: 10.3390/v4061011
pubmed: 22816037
King A.M.Q.; Adams M.J.; Carstens E.B.; Lefkowitz E.J.; Virus Taxonomy Ninth report of the International Committee on Taxonomy of Viruses 2012,486-487
Simmonds P.; Adams M.J.; Benkő M.; Breitbart M.; Brister J.R.; Carstens E.B.; Davison A.J.; Delwart E.; Gorbalenya A.E.; Harrach B.; Hull R.; King A.M.Q.; Koonin E.V.; Krupovic M.; Kuhn J.H.; Lefkowitz E.J.; Nibert M.L.; Orton R.; Roossinck M.J.; Sabanadzovic S.; Sullivan M.B.; Suttle C.A.; Tesh R.B.; van der Vlugt R.A.; Varsani A.; Zerbini F.M.; Virus taxonomy in the age of metagenomics. Nat Rev Microbiol 2017,15(3),161-168
doi: 10.1038/nrmicro.2016.177
pubmed: 28134265
Adams M.J.; Lefkowitz E.J.; King A.M.Q.; Harrach B.; Harrison R.L.; Knowles N.J.; Kropinski A.M.; Krupovic M.; Kuhn J.H.; Mushegian A.R.; Nibert M.L.; Sabanadzovic S.; Sanfaçon H.; Siddell S.G.; Simmonds P.; Varsani A.; Zerbini F.M.; Orton R.J.; Smith D.B.; Gorbalenya A.E.; Davison A.J.; 50 years of the international committee on taxonomy of viruses: Progress and prospects. Arch Virol 2017,162(5),1441-1446
doi: 10.1007/s00705-016-3215-y
pubmed: 28078475
Hilgenfeld R.; From SARS to MERS: Crystallographic studies on coronaviral proteases enable antiviral drug design. FEBS J 2014,281(18),4085-4096
doi: 10.1111/febs.12936
pubmed: 25039866
McBride R.; van Zyl M.; Fielding B.; The coronavirus nucleocapsid is a multifunctional protein. Viruses 2014,6(8),2991-3018
doi: 10.3390/v6082991
pubmed: 25105276
Guo Y.; Korteweg C.; McNutt M.A.; Gu J.; Pathogenetic mechanisms of severe acute respiratory syndrome. Virus Res 2008,133(1),4-12
doi: 10.1016/j.virusres.2007.01.022
pubmed: 17825937
Gallagher T.M.; Buchmeier M.J.; Coronavirus spike proteins in viral entry and pathogenesis. Virology 2001,279(2),371-374
doi: 10.1006/viro.2000.0757
pubmed: 11162792
Li F.; Structure, function, and evolution of coronavirus spike proteins. Annu Rev Virol 2016,3(1),237-261
doi: 10.1146/annurev-virology-110615-042301
pubmed: 27578435
Yuan Y.; Cao D.; Zhang Y.; Ma J.; Qi J.; Wang Q.; Lu G.; Wu Y.; Yan J.; Shi Y.; Zhang X.; Gao G.F.; Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. Nat Commun 2017,8(1),15092
doi: 10.1038/ncomms15092
pubmed: 28393837
Du L.; He Y.; Zhou Y.; Liu S.; Zheng B.J.; Jiang S.; The spike protein of SARS-CoV — a target for vaccine and therapeutic development. Nat Rev Microbiol 2009,7(3),226-236
doi: 10.1038/nrmicro2090
pubmed: 19198616
Prabakaran P.; Xiao X.; Dimitrov D.S.; A model of the ACE2 structure and function as a SARS-CoV receptor. Biochem Biophys Res Commun 2004,314(1),235-241
doi: 10.1016/j.bbrc.2003.12.081
pubmed: 14715271
Li W.; Moore M.J.; Vasilieva N.; Sui J.; Wong S.K.; Berne M.A.; Somasundaran M.; Sullivan J.L.; Luzuriaga K.; Greenough .C.; Choe H.; Farzan M.; Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 2003,426(6965),450-454
doi: 10.1038/nature02145
pubmed: 14647384
Jeffers S.A.; Tusell S.M.; Gillim-Ross L.; Hemmila E.M.; Achenbach J.E.; Babcock G.J.; Thomas W.D.; Thackray L.B.; Young M.D.; Mason R.J.; Ambrosino D.M.; Wentworth D.E.; DeMartini J.C.; Holmes K.V.; CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc Natl Acad Sci USA 2004,101(44),15748-15753
doi: 10.1073/pnas.0403812101
pubmed: 15496474
Yang Z.Y.; Huang Y.; Ganesh L.; Leung K.; Kong W.P.; Schwartz O.; Subbarao K.; Nabel G.J.; pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J Virol 2004,78(11),5642-5650
doi: 10.1128/JVI.78.11.5642-5650.2004
pubmed: 15140961
Han D.P.; Lohani M.; Cho M.W.; Specific asparagine-linked glycosylation sites are critical for DC-SIGN- and L-SIGNmediated severe acute respiratory syndrome coronavirus entry. J Virol 2007,81(21),12029-12039
doi: 10.1128/JVI.00315-07
pubmed: 17715238
Castaño-Rodriguez C.; Honrubia J.M.; Gutiérrez-Álvarez J.; DeDiego M.L.; Nieto-Torres J.L.; Jimenez-Guardeño J.M.; Regla-Nava J.A.; Fernandez-Delgado R.; Verdia-Báguena C.; Queralt-Martín M.; Kochan G.; Perlman S.; Aguilella V.M.; Sola I.; Enjuanes L.; Role of severe acute respiratory syndrome coronavirus viroporins E, 3a, and 8a in peplication and pathogenesis. MBio 2018,9(3),e02325-17
doi: 10.1128/mBio.02325-17
pubmed: 29789363
Kuo L.; Hurst K.R.; Masters P.S.; Exceptional flexibility in the sequence requirements for coronavirus small envelope protein function. J Virol 2007,81(5),2249-2262
doi: 10.1128/JVI.01577-06
pubmed: 17182690
Venkatagopalan P.; Daskalova S.M.; Lopez L.A.; Dolezal K.A.; Hogue B.G.; Coronavirus envelope (E) protein remains at the site of assembly. Virology 2015,478,75-85
doi: 10.1016/j.virol.2015.02.005
pubmed: 25726972
Schoeman D.; Fielding B.C.; Coronavirus envelope protein: Current knowledge. Virol J 2019,16(1),69
doi: 10.1186/s12985-019-1182-0
pubmed: 31133031
Arbely E.; Khattari Z.; Brotons G.; Akkawi M.; Salditt T.; Arkin I.T.; A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein. J Mol Biol 2004,341(3),769-779
doi: 10.1016/j.jmb.2004.06.044
pubmed: 15288785
Pervushin K.; Tan E.; Parthasarathy K.; Lin X.; Jiang F.L.; Yu D.; Vararattanavech A.; Soong T.W.; Liu D.X.; Torres J.; Structure and inhibition of the SARS coronavirus envelope protein ion channel. PLoS Pathog 2009,5(7),e1000511
doi: 10.1371/journal.ppat.1000511
pubmed: 19593379
Hogue B.G.; Machamer C.E.; Coronavirus structural proteins and virus assembly. Nidoviruses 2008,2008,179-200
Arndt A.L.; Larson B.J.; Hogue B.G.; A conserved domain in the coronavirus membrane protein tail is important for virus assembly. J Virol 2010,84(21),11418-11428
doi: 10.1128/JVI.01131-10
pubmed: 20719948
Wang Y.; Liu L.; The membrane protein of severe acute respiratory syndrome coronavirus functions as a novel cytosolic pathogen-associated molecular pattern to promote beta interferon induction via a toll-like-receptor-related TRAF3-independent mechanism. MBio 2016,7(1),e01872-15
doi: 10.1128/mBio.01872-15
pubmed: 26861016
Chang C.; Lo S.C.; Wang Y.S.; Hou M.H.; Recent insights into the development of therapeutics against coronavirus diseases by targeting N protein. Drug Discov Today 2016,21(4),562-572
doi: 10.1016/j.drudis.2015.11.015
pubmed: 26691874
Lin S.Y.; Liu C.L.; Chang Y.M.; Zhao J.; Perlman S.; Hou M.H.; Structural basis for the identification of the N-terminal domain of coronavirus nucleocapsid protein as an antiviral target. J Med Chem 2014,57(6),2247-2257
doi: 10.1021/jm500089r
pubmed: 24564608
Chang C.; Hou M.H.; Chang C.F.; Hsiao C.D.; Huang T.; The SARS coronavirus nucleocapsid protein - forms and functions. Antiviral Res 2014,103,39-50
doi: 10.1016/j.antiviral.2013.12.009
pubmed: 24418573
Zhou B.; Liu J.; Wang Q.; Liu X.; Li X.; Li P.; Ma Q.; Cao C.; The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha. J Virol 2008,82(14),6962-6971
doi: 10.1128/JVI.00133-08
pubmed: 18448518
Lo Y.S.; Lin S.Y.; Wang S.M.; Wang C.T.; Chiu Y.L.; Huang T.H.; Hou M.H.; Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein. FEBS Lett 2013,587(2),120-127
doi: 10.1016/j.febslet.2012.11.016
pubmed: 23178926
Lindner H.A.; Fotouhi-Ardakani N.; Lytvyn V.; Lachance P.; Sulea T.; Ménard R.; The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J Virol 2005,79(24),15199-15208
doi: 10.1128/JVI.79.24.15199-15208.2005
pubmed: 16306591
Jo S.; Kim S.; Shin D.H.; Kim M.S.; Inhibition of SARS-CoV 3CL protease by flavonoids. J Enzyme Inhib Med Chem 2020,35(1),145-151
doi: 10.1080/14756366.2019.1690480
pubmed: 31724441
Shimamoto Y.; Hattori Y.; Kobayashi K.; Teruya K.; Sanjoh A.; Nakagawa A.; Yamashita E.; Akaji K.; Fused-ring structure of decahydroisoquinolin as a novel scaffold for SARS 3CL protease inhibitors. Bioorg Med Chem 2015,23(4),876-890
doi: 10.1016/j.bmc.2014.12.028
pubmed: 25614110
Hu T.; Zhang Y.; Li L.; Wang K.; Chen S.; Chen J.; Ding J.; Jiang H.; Shen X.; Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure. Virology 2009,388(2),324-334
doi: 10.1016/j.virol.2009.03.034
pubmed: 19409595
Hsu M.F.; Kuo C.J.; Chang K.T.; Chang H.C.; Chou C.C.; Ko T.P.; Shr H.L.; Chang G.G.; Wang A.H.J.; Liang P.H.; Mechanism of the maturation process of SARS-CoV 3CL protease. J Biol Chem 2005,280(35),31257-31266
doi: 10.1074/jbc.M502577200
pubmed: 15788388
Barretto N.; Jukneliene D.; Ratia K.; Chen Z.; Mesecar A.D.; Baker S.C.; The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J Virol 2005,79(24),15189-15198
doi: 10.1128/JVI.79.24.15189-15198.2005
pubmed: 16306590
Han Y.S.; Chang G.G.; Juo C.G.; Lee H.J.; Yeh S.H.; Hsu J.T.A.; Chen X.; Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): Expression, purification, characterization, and inhibition. Biochemistry 2005,44(30),10349-10359
doi: 10.1021/bi0504761
pubmed: 16042412
Zeng Q.; Langereis M.A.; van Vliet A.L.W.; Huizinga E.G.; de Groot R.J.; Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proc Natl Acad Sci USA 2008,105(26),9065-9069
doi: 10.1073/pnas.0800502105
pubmed: 18550812
Frick D.; Lam A.; Understanding helicases as a means of virus control. Curr Pharm Des 2006,12(11),1315-1338
doi: 10.2174/138161206776361147
pubmed: 16611118
Karpe Y.A.; Lole K.S.; NTPase and 5′ to 3′ RNA duplex-unwinding activities of the hepatitis E virus helicase domain. J Virol 2010,84(7),3595-3602
doi: 10.1128/JVI.02130-09
pubmed: 20071563
Banerjee T.; Aggarwal M.; Sommers J.A.; Brosh R.M.; Biochemical and cell biological assays to identify and characterize DNA helicase inhibitors. Methods 2016,108,130-141
doi: 10.1016/j.ymeth.2016.04.007
pubmed: 27064001
Frieman M.; Yount B.; Agnihothram S.; Page C.; Donaldson E.; Roberts A.; Vogel L.; Woodruff B.; Scorpio D.; Subbarao K.; Baric R.S.; Molecular determinants of severe acute respiratory syndrome coronavirus pathogenesis and virulence in young and aged mouse models of human disease. J Virol 2012,86(2),884-897
doi: 10.1128/JVI.05957-11
pubmed: 22072787
Egloff M.P.; Ferron F.; Campanacci V.; Longhi S.; Rancurel C.; Dutartre H.; Snijder E.J.; Gorbalenya A.E.; Cambillau C.; Canard B.; The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc Natl Acad Sci USA 2004,101(11),3792-3796
doi: 10.1073/pnas.0307877101
pubmed: 15007178
Sutton G.; Fry E.; Carter L.; Sainsbury S.; Walter T.; Nettleship J.; Berrow N.; Owens R.; Gilbert R.; Davidson A.; Siddell S.; Poon L.L.M.; Diprose J.; Alderton D.; Walsh M.; Grimes J.M.; Stuart D.I.; The nsp9 replicase protein of SARS-coronavirus, structure and functional insights. Structure 2004,12(2),341-353
doi: 10.1016/j.str.2004.01.016
pubmed: 14962394
Ponnusamy R.; Moll R.; Weimar T.; Mesters J.R.; Hilgenfeld R.; Variable oligomerization modes in coronavirus non-structural protein 9. J Mol Biol 2008,383(5),1081-1096
doi: 10.1016/j.jmb.2008.07.071
pubmed: 18694760
Kirchdoerfer R.N.; Ward A.B.; Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat Commun 2019,10(1),2342
doi: 10.1038/s41467-019-10280-3
pubmed: 31138817
Ahn D.G.; Choi J.K.; Taylor D.R.; Oh J.W.; Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates. Arch Virol 2012,157(11),2095-2104
doi: 10.1007/s00705-012-1404-x
pubmed: 22791111
Subissi L.; Posthuma C.C.; Collet A.; Zevenhoven-Dobbe J.C.; Gorbalenya A.E.; Decroly E.; Snijder E.J.; Canard B.; Imbert I.; One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc Natl Acad Sci USA 2014,111(37),E3900-E3909
doi: 10.1073/pnas.1323705111
pubmed: 25197083
McDonald S.M.; RNA synthetic mechanisms employed by diverse families of RNA viruses. Wiley Interdiscip Rev RNA 2013,4(4),351-367
doi: 10.1002/wrna.1164
pubmed: 23606593
Gao Y.; Yan L.; Huang Y.; Liu F.; Zhao Y.; Cao L.; Wang R.; Sun Q.; Ming Z.; Zhang L.; Ge J.; Zheng L.; Zhang Y.; Wang H.; Zhu Y.; Zhu C.; Hu T.; Hua T.; Zhang B.; Yang X.; Li J.; Yang H.; Liu Z.; Xu W.; Guddat L.W.; Wang Q.; Lou Z.; Rao Z.; Structure of the RNA-dependent RNA polymerase from COVID-19 virus. Science 2020,368,779-782
Yin W.; Mao C.; Luan X.; Shen D.D.; Shen Q.; Su H.; Wang X.; Zhou F.; Zhao W.; Gao M.; Chang S.; Xie Y.C.; Tian G.; Jiang H.W.; Tao S.C.; Shen J.; Jiang Y.; Jiang H.; Xu Y.; Zhang S.; Zhang Y.; Xu H.E.; Structural basis for inhibition of the RNAdependent RNA polymerase from SARS-CoV-2 by remdesivir. Science 1504,2020(368),1499e
Wang Q.; Wu J.; Wang H.; Gao Y.; Liu Q.; Mu A.; Ji W.; Yan L.; Zhu Y.; Zhu C.; Fang X.; Yang X.; Huang Y.; Gao H.; Liu F.; Ge J.; Sun Q.; Yang X.; Xu W.; Liu Z.; Yang H.; Lou Z.; Jiang B.; Guddat L.W.; Gong P.; Rao Z.; Structural basis for RNA replication by the SARS-CoV-2 polymerase. Cell 2020,182,417-428
doi: 10.1016/j.cell.2020.05.034
Nandi S.; Roy H.; Gummadi A.; Saxena A.K.; Exploring spike protein as potential target of novel coronavirus and to inhibit the viability utilizing natural agents. Curr Drug Targets 2021,22(17),2006-2020
doi: 10.2174/1389450122666210309105820
pubmed: 33687893
Maurya V.K.; Kumar S.; Prasad A.K.; Bhatt M.L.B.; Saxena S.K.; Structure-based drug designing for potential antiviral activity of selected natural products from Ayurveda against SARS-CoV-2 spike glycoprotein and its cellular receptor. Virusdisease 2020,31(2),179-193
doi: 10.1007/s13337-020-00598-8
pubmed: 32656311
Lelli D.; Sahebkar A.; Johnston T.P.; Pedone C.; Curcumin use in pulmonary diseases: State of the art and future perspectives. Pharmacol Res 2017,115,133-148
doi: 10.1016/j.phrs.2016.11.017
pubmed: 27888157
Jena A.B.; Kanungo N.; Nayak V.; Chainy G.B.N.; Dandapat J.; Catechin and curcumin interact with S protein of SARS-CoV2 and ACE2 of human cell membrane: Insights from computational studies. Sci Rep 2021,11(1),2043
doi: 10.1038/s41598-021-81462-7
pubmed: 33479401
Mhatre S.; Gurav N.; Shah M.; Patravale V.; Entry-inhibitory role of catechins against SARS-CoV-2 and its UK variant. Comput Biol Med 2021,135,104560
doi: 10.1016/j.compbiomed.2021.104560
pubmed: 34147855
Kumar G.; Kumar D.; Singh N.P.; Therapeutic Approach against 2019-nCoV by Inhibition of ACE-2 Receptor. Drug Res (Stuttg) 2021,71(4),213-218
doi: 10.1055/a-1275-0228
pubmed: 33184809
Marín-Palma D.; Tabares-Guevara J.H.; Zapata-Cardona M.I.; Flórez-Álvarez L.; Yepes L.M.; Rugeles M.T.; Zapata-Builes W.; Hernandez J.C.; Taborda N.A.; Curcumin inhibits in vitro SARS-CoV-2 infection in vero E6 cells through multiple antiviral mechanisms. Molecules 2021,26(22),6900
doi: 10.3390/molecules26226900
pubmed: 34833991
Udeinya I.J.; Mbah A.U.; Chijioke C.P.; Shu E.N.; An antimalarial extract from neem leaves is antiretroviral. Trans R Soc Trop Med Hyg 2004,98(7),435-437
doi: 10.1016/j.trstmh.2003.10.016
pubmed: 15138081
Biswas K.; Chattopadhyay I.; Banerjee R.K.; Bandyopadhyay U.; Biological activities and medicinal properties of neem (Azadirachta indica). Curr Sci 2002,82,1336-1345
Shadrack D.M.; Vuai S.A.H.; Sahini M.G.; Onoka I.; In silico study of the inhibition of SARS-COV-2 viral cell entry by neem tree extracts. RSC Advances 2021,11(43),26524-26533
doi: 10.1039/D1RA04197E
pubmed: 35480004
Sarkar L.; Oko L.; Gupta S.; Bubak A.N.; Das B.; Gupta P.; Safiriyu A.A.; Singhal C.; Neogi U.; Bloom D.; Banerjee A.; Mahalingam R.; Cohrs R.J.; Koval M.; Shindler K.S.; Pal D.; Nagel M.; Sarma J.D.; Azadirachta indica A. Juss bark extract and its Nimbin isomers restrict β-coronaviral infection and replication. Virology 2022,569,13-28
doi: 10.1016/j.virol.2022.01.002
pubmed: 35219218
Ye Q.; Wang B.; Mao J.; The pathogenesis and treatment of the ‘Cytokine Storm’ in COVID-19. J Infect 2020,80(6),607-613
doi: 10.1016/j.jinf.2020.03.037
pubmed: 32283152
Straughn A.R.; Kakar S.S.; Withaferin A.; A potential therapeutic agent against COVID-19 infection. J Ovarian Res 2020,13(1),79
doi: 10.1186/s13048-020-00684-x
pubmed: 32684166
Chikhale R.V.; Gurav S.S.; Patil R.B.; Sinha S.K.; Prasad S.K.; Shakya A.; Shrivastava S.K.; Gurav N.S.; Prasad R.S.; Sars-cov-2 host entry and replication inhibitors from Indian ginseng: An in-silico approach. J Biomol Struct Dyn 2021,39(12),4510-4521
pubmed: 32568012
Balkrishna A.; Pokhrel S.; Singh H.; Joshi M.; Mulay V.P.; Haldar S.; Varshney A.; Withanone from Withania somnifera Attenuates SARS-CoV-2 RBD and Host ACE2 Interactions to Rescue Spike Protein Induced Pathologies in Humanized Zebrafish Model. Drug Des Devel Ther 2021,15,1111-1133
doi: 10.2147/DDDT.S292805
pubmed: 33737804
Kim S.H.; Lee Y.C.; Piperine inhibits eosinophil infiltration and airway hyperresponsiveness by suppressing T cell activity and Th2 cytokine production in the ovalbumin-induced asthma model. J Pharm Pharmacol 2009,61(3),353-359
doi: 10.1211/jpp.61.03.0010
pubmed: 19222908
Rout J.; Swain B.C.; Tripathy U.; In silico investigation of spice molecules as potent inhibitor of SARS-CoV-2. J Biomol Struct Dyn 2021,40(2),860-874
pubmed: 32938313
Liu W.; Zhang X.; Liu P.; Shen X.; Lan T.; Li W.; Jiang Q.; Xie X.; Huang H.; Effects of berberine on matrix accumulation and NF-kappa B signal pathway in alloxan-induced diabetic mice with renal injury. Eur J Pharmacol 2010,638(1-3),150-155
doi: 10.1016/j.ejphar.2010.04.033
pubmed: 20447389
Wang Z.Z.; Li K.; Maskey A.R.; Huang W.; Toutov A.A.; Yang N.; Srivastava K.; Geliebter J.; Tiwari R.; Miao M.; Li X.M.; A small molecule compound berberine as an orally active therapeutic candidate against COVID‐19 and SARS: A computational and mechanistic study. FASEB J 2021,35(4),e21360
doi: 10.1096/fj.202001792R
pubmed: 33749932
Varghese F.; van Woudenbergh E.; Overheul G.; Eleveld M.; Kurver L.; van Heerbeek N.; van Laarhoven A.; Miesen P.; den Hartog G.; de Jonge M.; van Rij R.; Berberine and obatoclax inhibit SARS-Cov-2 replication in primary human nasal epithelial cells in vitro. Viruses 2021,13(2),282
doi: 10.3390/v13020282
pubmed: 33670363
Liu Y.T.; Chen H.W.; Lii C.K.; Jhuang J.H.; Huang C.S.; Li M.L.; Yao H.T.; A diterpenoid, 14-deoxy-11, 12-didehydroandrographolide, in Andrographis paniculata reduces steatohepatitis and liver injury in mice fed a high-fat and highcholesterol diet. Nutrients 2020,12(2),523
doi: 10.3390/nu12020523
Sa-ngiamsuntorn K.; Suksatu A.; Pewkliang Y.; Thongsri P.; Kanjanasirirat P.; Manopwisedjaroen S.; Charoensutthivarakul S.; Wongtrakoongate P.; Pitiporn S.; Chaopreecha J.; Kongsomros S.; Jearawuttanakul K.; Wannalo W.; Khemawoot P.; Chutipongtanate S.; Borwornpinyo S.; Thitithanyanont A.; Hongeng S.; Anti-SARS-CoV-2 activity of Andrographis paniculata extract and its major component Andrographolide in human lung epithelial cells and cytotoxicity evaluation in major organ cell representatives. J Nat Prod 2021,84(4),1261-1270
doi: 10.1021/acs.jnatprod.0c01324
pubmed: 33844528
Basu A.; Sarkar A.; Maulik U.; Molecular docking study of potential phytochemicals and their effects on the complex of SARS-CoV2 spike protein and human ACE2. Sci Rep 2020,10(1),17699
doi: 10.1038/s41598-020-74715-4
pubmed: 33077836
Vijayakumar B.G.; Ramesh D.; Joji A.; Jayachandra prakasan J.; Kannan T.; In silico pharmacokinetic and molecular docking studies of natural flavonoids and synthetic indole chalcones against essential proteins of SARS-CoV-2. Eur J Pharmacol 2020,886,173448
doi: 10.1016/j.ejphar.2020.173448
pubmed: 32768503
Bhowmik D.; Nandi R.; Prakash A.; Kumar D.; Evaluation of flavonoids as 2019-nCoV cell entry inhibitor through molecular docking and pharmacological analysis. Heylion 2021,7(3),E06515
Kreft S.; Knapp M.; Kreft I.; Extraction of rutin from buckwheat (Fagopyrum esculentum Moench) seeds and determination by capillary electrophoresis. J Agric Food Chem 1999,47(11),4649-4652
doi: 10.1021/jf990186p
pubmed: 10552865
Zhao Z.; Moghadasian M.H.; Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: A review. Food Chem 2008,109(4),691-702
doi: 10.1016/j.foodchem.2008.02.039
pubmed: 26049981
Kumar N.; Pruthi V.; Potential applications of ferulic acid from natural sources. Biotechnol Rep (Amst) 2014,4,86-93
doi: 10.1016/j.btre.2014.09.002
pubmed: 28626667
Bhowmik D.; Nandi R.; Jagadeesan R.; Kumar N.; Prakash A.; Kumar D.; Identification of potential inhibitors against SARS-CoV-2 by targeting proteins responsible for envelope formation and virion assembly using docking based virtual screening, and pharmacokinetics approaches. Infect Genet Evol 2020,84,104451
doi: 10.1016/j.meegid.2020.104451
pubmed: 32640381
Khuda-Bukhsh A.R.; Das J.; Samadder A.; Das S.; Paul A.; Nanopharmaceutical approach for enhanced anti-cancer activity of betulinic acid in lung-cancer treatment via activation of PARP: Interaction with dna as a target:-anti-cancer. J Pharmacopuncture 2016,19(1),37-44
doi: 10.3831/KPI.2016.19.005
pubmed: 27280048
Mandal A.; Jha A.K.; Hazra B.; Plant products as inhibitors of coronavirus 3CL protease. Front Pharmacol 2021,12,583387
doi: 10.3389/fphar.2021.583387
pubmed: 33767619
Rastogi S.; Pandey M.M.; Kumar Singh Rawat A.; Medicinal plants of the genus Betula—Traditional uses and a phytochemical–pharmacological review. J Ethnopharmacol 2015,159,62-83
doi: 10.1016/j.jep.2014.11.010
pubmed: 25449458
Das J.; Das S.; Samadder A.; Bhadra K.; Khuda-Bukhsh A.R.; Poly (lactide-co-glycolide) encapsulated extract of Phytolacca decandra demonstrates better intervention against induced lung adenocarcinoma in mice and on A549 cells. Eur J Pharm Sci 2012,47(2),313-324
doi: 10.1016/j.ejps.2012.06.018
pubmed: 22771545
Das J.; Das S.; Paul A.; Samadder A.; Khuda-Bukhsh A.R.; Strong anticancer potential of nano-triterpenoid from Phytolacca decandra against A549 adenocarcinoma via a Ca2+-dependent mitochondrial apoptotic pathway. J Acupunct Meridian Stud 2014,7(3),140-150
doi: 10.1016/j.jams.2013.07.009
pubmed: 24929458
Jäger S.; Laszczyk M.; Scheffler A.; A preliminary pharmacokinetic study of betulin, the main pentacyclic triterpene from extract of outer bark of birch (Betulae alba cortex). Molecules 2008,13(12),3224-3235
doi: 10.3390/molecules13123224
pubmed: 19104487
Bildziukevich U.; Özdemir Z.; Wimmer Z.; Recent achievements in medicinal and supramolecular chemistry of betulinic acid and its derivatives. Molecules 2019,24(19),3546
doi: 10.3390/molecules24193546
pubmed: 31574991
Wen C.C.; Kuo Y.H.; Jan J.T.; Liang P.H.; Wang S.Y.; Liu H.G.; Lee C.K.; Chang S.T.; Kuo C.J.; Lee S.S.; Hou C.C.; Hsiao P.W.; Chien S.C.; Shyur L.F.; Yang N.S.; Specific plant terpenoids and lignoids possess potent antiviral activities against severe acute respiratory syndrome coronavirus. J Med Chem 2007,50(17),4087-4095
doi: 10.1021/jm070295s
pubmed: 17663539
Pillaiyar T.; Manickam M.; Namasivayam V.; Hayashi Y.; Jung S.H.; An overview of severe acute respiratory syndrome–coronavirus (SARS-CoV) 3CL protease inhibitors: Peptidomimetics and small molecule chemotherapy. J Med Chem 2016,59(14),6595-6628
doi: 10.1021/acs.jmedchem.5b01461
pubmed: 26878082
Verma S.; Twilley D.; Esmear T.; Oosthuizen C.B.; Reid A.M.; Nel M.; Lall N.; Anti-SARS-CoV natural products with the potential to inhibit SARS-CoV-2 (COVID-19). Front Pharmacol 2020,11,561334
doi: 10.3389/fphar.2020.561334
pubmed: 33101023
Kim D.W.; Seo K.H.; Curtis-Long M.J.; Oh K.Y.; Oh J.W.; Cho J.K.; Lee K.H.; Park K.H.; Phenolic phytochemical displaying SARS-CoV papain-like protease inhibition from the seeds of Psoralea corylifolia. J Enzyme Inhib Med Chem 2014,29(1),59-63
doi: 10.3109/14756366.2012.753591
pubmed: 23323951
Ryu Y.B.; Jeong H.J.; Kim J.H.; Kim Y.M.; Park J.Y.; Kim D.; Naguyen T.T.H.; Park S.J.; Chang J.S.; Park K.H.; Rho M-C.; Lee W.S.; Biflavonoids from Torreya nucifera displaying SARS-CoV 3CLpro inhibition. Bioorg Med Chem 2010,18(22),7940-7947
doi: 10.1016/j.bmc.2010.09.035
pubmed: 20934345
Hamburger M.; Isatis tinctoria – From the rediscovery of an ancient medicinal plant towards a novel anti-inflammatory phytopharmaceutical. Phytochem Rev 2002,1(3),333-344
doi: 10.1023/A:1026095608691
Lin C.W.; Tsai F.J.; Tsai C.H.; Lai C.C.; Wan L.; Ho T.Y.; Hsieh C.C.; Chao P.D.L.; Anti-SARS coronavirus 3C-like protease effects of Isatis indigotica root and plant-derived phenolic compounds. Antiviral Res 2005,68(1),36-42
doi: 10.1016/j.antiviral.2005.07.002
pubmed: 16115693
Murakami S.; Kotomo S.; Ozawa M.; Baba K.; Novel chalcone derivative as antiulcer agent. Patent Japan Kokai Koho 04 1992
Fujita T.; Sakuma S.; Sumiya T.; Nishida H.; Fujimoto Y.; Baba K.; Kozawa M.; The effects of xanthoangelol E on arachidonic acid metabolism in the gastric antral mucosa and platelet of the rabbit. Res Commun Chem Pathol Pharmacol 1992,77(2),227-240
pubmed: 1439191
Matsuura M.; Kimura Y.; Nakata K.; Baba K.; Okuda H.; Artery relaxation by chalcones isolated from the roots of Angelica keiskei. Planta Med 2001,67(3),230-235
doi: 10.1055/s-2001-12011
pubmed: 11345693
Nakata K.; Baba K.; Histamine release-inhibiting activity of Angelica keiskei. Nat Med 2001,55,32-34
Kil Y.S.; Pham S.T.; Seo E.K.; Jafari M.; Angelica keiskei, an emerging medicinal herb with various bioactive constituents and biological activities. Arch Pharm Res 2017,40(6),655-675
doi: 10.1007/s12272-017-0892-3
pubmed: 28439780
Park J.Y.; Ko J.A.; Kim D.W.; Kim Y.M.; Kwon H.J.; Jeong H.J.; Kim C.Y.; Park K.H.; Lee W.S.; Ryu Y.B.; Chalcones isolated from Angelica keiskei inhibit cysteine proteases of SARS-CoV. J Enzyme Inhib Med Chem 2016,31(1),23-30
doi: 10.3109/14756366.2014.1003215
pubmed: 25683083
Shree P.; Mishra P.; Selvaraj C.; Singh S.K.; Chaube R.; Garg N.; Tripathi Y.B.; Targeting COVID-19 (SARS-CoV-2) main protease through active phytochemicals of ayurvedic medicinal plants – Withania somnifera (Ashwagandha), Tinospora cordifolia (Giloy) and Ocimum sanctum (Tulsi) – a molecular docking study. J Biomol Struct Dyn 2022,40(1),190-203
doi: 10.1080/07391102.2020.1810778
pubmed: 32851919
Murugesan S.; Kottekad S.; Crasta I.; Sreevathsan S.; Usharani D.; Perumal M.K.; Mudliar S.N.; Targeting COVID-19 (SARS-CoV-2) main protease through active phytocompounds of ayurvedic medicinal plants – Emblica officinalis (Amla), Phyllanthus niruri Linn. (Bhumi Amla) and Tinospora cordifolia (Giloy) – A molecular docking and simulation study. Comput Biol Med 2021,136,104683
doi: 10.1016/j.compbiomed.2021.104683
pubmed: 34329860
Aanouz I.; Belhassan A.; El-Khatabi K.; Lakhlifi T.; El-ldrissi M.; Bouachrine M.; Moroccan medicinal plants as inhibitors against SARS-CoV-2 main protease: Computational investigations. J Biomol Struct Dyn 2021,39(8),2971-2979
doi: 10.1080/07391102.2020.1758790
pubmed: 32306860
Ngo S.T.; Quynh Anh Pham N.; Thi Le L.; Pham D.H.; Vu V.V.; Computational determination of potential inhibitors of SARS-CoV-2 Main Protease. J Chem Inf Model 2020,60(12),5771-5780
doi: 10.1021/acs.jcim.0c00491
pubmed: 32530282
Khan A.; Ali S.S.; Khan M.T.; Saleem S.; Ali A.; Suleman M.; Babar Z.; Shafiq A.; Khan M.; Wei D.Q.; Combined drug repurposing and virtual screening strategies with molecular dynamics simulation identified potent inhibitors for SARS-CoV-2 main protease (3CLpro). J Biomol Struct Dyn 2021,39(13),4659-4670
doi: 10.1080/07391102.2020.1779128
pubmed: 32552361
Khan A.; Heng W.; Wang Y.; Qiu J.; Wei X.; Peng S.; Saleem S.; Khan M.; Ali S.S.; Wei D.Q.; In silico and in vitro evaluation of kaempferol as a potential inhibitor of the SARS‐COV‐2 main protease (3CLPRO). Phytother Res 2021,35(6),2841-2845
doi: 10.1002/ptr.6998
pubmed: 33448101
Nguyen T.T.H.; Woo H.J.; Kang H.K.; Nguyen V.D.; Kim Y.M.; Kim D.W.; Ahn S.A.; Xia Y.; Kim D.; Flavonoid-mediated inhibition of SARS coronavirus 3C-like protease expressed in Pichia pastoris. Biotechnol Lett 2012,34(5),831-838
doi: 10.1007/s10529-011-0845-8
pubmed: 22350287
Ghosh R.; Chakraborty A.; Biswas A.; Chowdhuri D.S.; Evaluation of green tea polyphenols as novel corona virus (SARS CoV-2) main protease (Mpro) inhibitors – an in silico docking and molecular dynamics simulation study. J Biomol Struct Dyn ,39(12),4362-4374
pubmed: 32568613
Kar P.; Kumar V.; Vellingiri B.; Sen A.; Jaishee N.; Anandraj A.; Malhotra H.; Bhattacharyya S.; Mukhopadhyay S.; Kinoshita M.; Govindasamy V.; Anisotine and amarogentin as promising inhibitory candidates against SARS-CoV-2 proteins: A computational investigation. J Biomol Struct Dyn 2022,40(10),4532-4542
pubmed: 33305988
Gentile D.; Patamia V.; Scala A.; Sciortino M.T.; Piperno A.; Rescifina A.; Putative inhibitors of SARS-CoV-2 main protease from a library of marine natural products: A virtual screening and molecular modeling study. Mar Drugs 2020,18(4),225
doi: 10.3390/md18040225
pubmed: 32340389
Vivek-Ananth R.P.; Krishnaswamy S.; Samal A.; Potential phytochemical inhibitors of SARS-CoV-2 helicase Nsp13: A molecular docking and dynamic simulation study. Mol Divers 2022,26(1),429-442
doi: 10.1007/s11030-021-10251-1
pubmed: 34117992
Häkkinen S.H.; Kärenlampi S.O.; Heinonen I.M.; Mykkänen H.M.; Törrönen A.R.; Content of the flavonols quercetin, myricetin, and kaempferol in 25 edible berries. J Agric Food Chem 1999,47(6),2274-2279
doi: 10.1021/jf9811065
pubmed: 10794622
Miean K.H.; Mohamed S.; Flavonoid (myricetin, quercetin, kaempferol, luteolin, and apigenin) content of edible tropical plants. J Agric Food Chem 2001,49(6),3106-3112
doi: 10.1021/jf000892m
pubmed: 11410016
Yu M.S.; Lee J.; Lee J.M.; Kim Y.; Chin Y.W.; Jee J.G.; Keum Y.S.; Jeong Y.J.; Identification of myricetin and scutellarein as novel chemical inhibitors of the SARS coronavirus helicase, nsP13. Bioorg Med Chem Lett 2012,22(12),4049-4054
doi: 10.1016/j.bmcl.2012.04.081
pubmed: 22578462
Mani J.S.; Johnson J.B.; Steel J.C.; Broszczak D.A.; Neilsen P.M.; Walsh K.B.; Naiker M.; Natural product-derived phytochemicals as potential agents against coronaviruses: A review. Virus Res 2020,284,197989
doi: 10.1016/j.virusres.2020.197989
pubmed: 32360300
Yang Z.F.; Bai L.P.; Huang W.; Li X.Z.; Zhao S.S.; Zhong N.S.; Jiang Z.H.; Comparison of in vitro antiviral activity of tea polyphenols against influenza A and B viruses and structure–activity relationship analysis. Fitoterapia 2014,93,47-53
doi: 10.1016/j.fitote.2013.12.011
pubmed: 24370660
Chowdhury P.; Sahuc M.E.; Rouillé Y.; Rivière C.; Bonneau N.; Vandeputte A.; Brodin P.; Goswami M.; Bandyopadhyay T.; Dubuisson J.; Séron K.; Theaflavins, polyphenols of black tea, inhibit entry of hepatitis C virus in cell culture. PLoS One 2018,13(11),e0198226
doi: 10.1371/journal.pone.0198226
pubmed: 30485282
Lung J.; Lin Y.S.; Yang Y.H.; Chou Y.L.; Shu L.H.; Cheng Y.C.; Liu H.T.; Wu C.Y.; The potential chemical structure of anti‐SARS‐CoV‐2 RNA‐dependent RNA polymerase. J Med Virol 2020,92(6),693-697
doi: 10.1002/jmv.25761
pubmed: 32167173
Singh S.; Md Sk F.; Sonawane A.; Kar P.; Sadhukhan S.; Plant-derived natural polyphenols as potential antiviral drugs against SARS-CoV-2 via RNA-dependent RNA polymerase (RdRp) inhibition: An in-silico analysis. J Biomol Struct Dyn 2020
pubmed: 32720577
Ahmed-Belkacem A.; Guichou J.F.; Brillet R.; Ahnou N.; Hernandez E.; Pallier C.; Pawlotsky J.M.; Inhibition of RNA binding to hepatitis C virus RNA-dependent RNA polymerase: A new mechanism for antiviral intervention. Nucleic Acids Res 2014,42(14),9399-9409
doi: 10.1093/nar/gku632
pubmed: 25053847
Koulgi S.; Jani V.; Uppuladinne V.N, M.; Sonavane U.; Joshi R.; Natural plant products as potential inhibitors of RNA dependent RNA polymerase of severe acute respiratory syndrome coronavirus-2. PLoS One 2021,16(5),e0251801
doi: 10.1371/journal.pone.0251801
pubmed: 33984041
Molavi Z.; Razi S.; Mirmotalebisohi S.A.; Adibi A.; Sameni M.; Karami F.; Niazi V.; Niknam Z.; Aliashrafi M.; Taheri M.; Ghafouri-Fard S.; Jeibouei S.; Mahdian S.; Zali H.; Ranjbar M.M.; Yazdani M.; Identification of FDA approved drugs against SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and 3-chymotrypsin-like protease (3CLpro), drug repurposing approach. Biomed Pharmacother 2021,138,111544
doi: 10.1016/j.biopha.2021.111544
pubmed: 34311539
Borquaye L.S.; Gasu E.N.; Ampomah G.B.; Kyei L.K.; Amarh M.A.; Mensah C.N.; Nartey D.; Commodore M.; Adomako A.K.; Acheampong P.; Mensah J.O.; Mormor D.B.; Aboagye C.I.; Alkaloids from Cryptolepis sanguinolenta as potential inhibitors of SARS-CoV-2 viral proteins: An in silico study. BioMed Res Int 2020,2020,5324560
doi: 10.1155/2020/5324560
pubmed: 33029513
Bhardwaj V.K.; Singh R.; Sharma J.; Rajendran V.; Purohit R.; Kumar S.; Identification of bioactive molecules from Tea plant as SARS-CoV-2 main protease inhibitors. J Biomol Struct Dyn 2020,39(10),3449-3458
pubmed: 32397940
Cory H.; Passarelli S.; Szeto J.; Tamez M.; Mattei J.; The role of polyphenols in human health and food systems: A mini-review. Front Nutr 2018,5,87
doi: 10.3389/fnut.2018.00087
pubmed: 30298133
Kushwaha P.P.; Singh A.K.; Bansal T.; Yadav A.; Prajapati K.S.; Shuaib M.; Kumar S.; Identification of natural inhibitors against SARS-CoV-2 drugable targets using molecular docking, molecular dynamics simulation, and MM-PBSA approach. Front Cell Infect Microbiol 2021,11,730288
doi: 10.3389/fcimb.2021.730288
pubmed: 34458164
Srikanth L.; Sarma P.V.G.K.; Andrographolide binds to spike glycoprotein and RNA-dependent RNA polymerase (NSP12) of SARS-CoV-2 by in silico approach: A probable molecule in the development of anti-coronaviral drug. J Genet Eng Biotechnol 2021,19(1),101
doi: 10.1186/s43141-021-00201-7
pubmed: 34255214
Enmozhi S.K.; Raja K.; Sebastine I.; Joseph J.; Andrographolide as a potential inhibitor of SARS-CoV-2 main protease: An in silico approach. J Biomol Struct Dyn 2020,1-7
doi: 10.1080/07391102.2020.1760136
pubmed: 32329419
Carneiro B.M.; Batista M.N.; Braga A.C.S.; Nogueira M.L.; Rahal P.; The green tea molecule EGCG inhibits Zika virus entry. Virology 2016,496,215-218
doi: 10.1016/j.virol.2016.06.012
pubmed: 27344138
Moon Y.J.; Morris M.E.; Pharmacokinetics and bioavailability of the bioflavonoid biochanin A: Effects of quercetin and EGCG on biochanin A disposition in rats. Mol Pharm 2007,4(6),865-872
doi: 10.1021/mp7000928
pubmed: 17970592
Xiao T.; Cui M.; Zheng C.; Wang M.; Sun R.; Gao D.; Bao J.; Ren S.; Yang B.; Lin J.; Li X.; Li D.; Yang C.; Zhou H.; Myricetin inhibits SARS-CoV-2 viral replication by targeting Mpro and ameliorates pulmonary inflammation. Front Pharmacol 2021,12,669642
doi: 10.3389/fphar.2021.669642
pubmed: 34220507
da Silva F.M.A.; da Silva K.P.A.; de Oliveira L.P.M.; Costa E.V.; Koolen H.H.F.; Pinheiro M.L.B.; de Souza A.Q.L.; de Souza A.D.L.; Flavonoid glycosides and their putative human metabolites as potential inhibitors of the SARS-CoV-2 main protease (Mpro) and RNA-dependent RNA polymerase (RdRp). Mem Inst Oswaldo Cruz 2020,115,e200207
doi: 10.1590/0074-02760200207
pubmed: 33027419