The Antiviral Activity of Andrographolide, the Active Metabolite from Andrographis paniculata (Burm. f.) Wall. ex Nees. against SARS-CoV-2 by Using Bio- and Chemoinformatic Tools
Keywords:Antiviral activity, SARS-CoV-2, Andrographolide, Andrographis paniculata, Computational techniques
Due to the severe acute respiratory syndrome coronavirus 2 or SARS-CoV-2 outbreak, the virus has been wildly spread throughout the world and the number of infected patients has rapidly increased. More importantly, neither the official drug treatment nor the vaccine has been officially offered. These have considerably increased the public concerns internationally and nationally. Recently, there has been one question raised in the Thai society; “Could a common Thai herbal medicine namely Andrographis paniculata be used against SARS-CoV-2 infection?”. It is well-known that the plant has antiviral properties against wild ranges of viruses and the active metabolite is andrographolide. To date, there have only been a few studies investigating the anti-SARS-CoV-2 activity from andrographolide. To provide a better understanding, this study was conducted by applying the advanced techniques in both computational biology and chemistry to evaluate the anti-SARS-CoV-2 potential of andrographolide. In this study, andrographolide was tested against two key enzymes of SAR-CoV-2 namely 3C main proteinase and RNA dependent RNA polymerase. The result here indicated that andrographolide could only inhibit the SARS-CoV-2 3C main proteinase as strong as lopinavir (the standard medicine), which has been recommended as the drug of choice to treat SARS-CoV-2 patient.
FA Rabi, MSA Zoubi, GA Kasasbeh, DM Salameh and ADA Nasser. SARS-CoV-2 and coronavirus disease 2019: What we know so far. Pathogens 2020; 9, 231.
RA Neher, RA Dyrdak,V Druelle, EB Hodcroft and J Albert. Potential impact of seasonal forcing on a SARS-CoV-2 pandemic. Swiss. Med. Wkly. 2020; 150, 1-8.
Y Zhou, Y Hou, J Shen, Y Huang, W Martin and F Cheng. Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2. Cell. Discov. 2020; 6, 14.
S Gupta, KP Mishra and L Ganju. Broad-spectrum antiviral properties of andrographolide. Arch. Virol. 2017; 162, 611-23.
M Macchiagodena, M Pagliai and P Procacci. Inhibition of the main protease 3CL-pro of the Coronavirus Disease 19 via structure-based ligand design and molecular modeling. arXiv. preprint. 2020. https://doi.org/arXiv:2002.09937.
AC Walls, YJ Park, MA Tortorici, A Wall, AT McGuire and D Veesler. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 2020; 181, 281-92.
MA Phillips, MA Stewart, DL Woodling and ZR Xie. Has molecular docking ever brought us a medicine. Molecular Docking. IntechOpen, London, UK, 2018, p. 141-78.
X Zhu, Q Liu, L Du, L Lu and S Jiang. Receptor-binding domain as a target for developing SARS vaccines. J. Thorac. Dis. 2013; 5, 142-8.
Notepad++, Available at: https://notepad-plus-plus.org, accessed March 2020.
M Gouy, S Guindon and O Gascuel. SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol. Biol. Evol. 2010; 27, 221-4.
S Chetty and ME Soliman. Possible allosteric binding site on Gyrase B, a key target for novel anti-TB drugs: Homology modelling and binding site identification using molecular dynamics simulation and binding free energy calculations. Med. Chem. Res. 2015; 24, 2055-74.
EF Pettersen, TD Goddard, CC Huang, GS Couch, DM Greenblatt, EC Meng and TE Ferrin. UCSF Chimera--a visualization system for exploratory research and analysis. J. Comput. Chem. 2004; 25, 1605-12.
O Trott and AJ Olson. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J. Comput. Chem. 2010; 31, 455-61.
AD Hunter. ACD/ChemSketch 1.0 (freeware); ACD/ChemSketch 2.0 and its tautomers, dictionary, and 3D plug-ins; ACD/HNMR 2.0; ACD/CNMR 2.0. J. Chem. Educ. 1997; 74, 905-6
MD Hanwell, DE Curtis, DC Lonie, T Vandermeersch, E Zurek and GR Hutchison. Avogadro: An advanced semantic chemical editor, visualization, and analysis platform. J. Cheminformatics. 2012; 4, 1-17.
JH Jiang and P Deng. Discovery of new inhibitors of transforming growth factor-beta type 1 receptor by utilizing docking and structure-activity relationship analysis. Int. J. Mol. Sci. 2019; 20, 4090.
L Zhang and R Zhou. Binding mechanism of remdesivir to SARS-CoV-2 RNA dependent RNA polymerase. Preprints 2020. https://doi.org/10.20944/preprints202003.0267.v1.
J Lung, YS Lin, YH Yang, YL Chou, LH Shu, YC Cheng, HT Liu and CY Wu. The potential chemical structure of anti‐SARS‐CoV‐2 RNA‐dependent RNA polymerase. J. Med. Virol. 2020; 92 693-7.
Z Jin, X Du, Y Xu, Y Deng, M Liu, Y Zhao, B Zhang, X Li, L Zhang, C Peng and Y Duan. Structure of M pro from SARS-CoV-2 and discovery of its inhibitors. Nature 2020; 582, 289-93.
C Wu, Y Liu, Y Yang, P Zhang, W Zhong, Y Wan, Q Wang, Y Xu, M Li, X Li and M Zheng. Analysis of therapeutic targets for SARS-CoV-2 and discovery of potential drugs by computational methods. Acta Pharm. Sin. B 2020; 10, 766-88.
V Chandramohan, A Kaphle, M Chekuri, S Gangarudraiah and GB Siddaiah. Evaluating andrographolide as a potent inhibitor of NS3-4A protease and its drug-resistant mutants using in silico approaches. Adv. Virol. 2015; 4, 1-9.
K Bafna, RM Krug and GT Montelione. Structural similarity of SARS-CoV-2 Mpro and HCV NS3/4A proteases suggests new approaches for identifying existing drugs useful as COVID-19 therapeutics. ChemRxiv 2020. https://dx.doi.org/10.26434%2Fchemrxiv.12153615.
RN Kirchdoerfer and AB Ward. Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat. Commun. 2019; 10, 2342.
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