International E-publication: Publish Projects, Dissertation, Theses, Books, Souvenir, Conference Proceeding with ISBN.  International E-Bulletin: Information/News regarding: Academics and Research

Docking Studies of Components of Tulsi and Mamejavo against Plasmodium Lactate Dehydrogenase

Author Affiliations

  • 1Dolat Usha Institute of Applied Sciences, Valsad; Veer Narmad South Gujarat University, Surat, Gujarat, INDIA
  • 2Shree Ram Krishna Institute of Comp. Edu. and Applied Sciences; Veer Narmad South Gujarat University, Surat, Gujarat, INDIA

Int. Res. J. Biological Sci., Volume 2, Issue (2), Pages 8-12, February,10 (2013)


WHO estimates rank malaria as one of the top three killers among infectious diseases. Though many drugs are available for treatment of malaria, malarial parasite especially Plasmodium falciparum quickly develops resistance under selective drug pressure. Hence we require an array of new drugs for malaria treatment. Lactate dehydrogenase (LDH) is an essential enzyme that catalyses the interconversion of pyruvate and lactate with concomitant conversion of NADH and NAD+ . Being an important enzyme of glycolysis for energy production it may prove good target for antimalarial drugs. In our study we retrieved Plasmodium LDH structures from PDB and used them as a drug target protein. Different structures of components of tulsi – Ocimum sanctum and mamejavo – Enicostema littorale were retrieved from PubChem and Zinc databases and docking was performed using Argus lab and Swissdock softwares. In this comparative study we found Argus lab more effective than Swissdock as it can give the results of e-value. Components of tulsi and mamejavo like apigenin, luteolin, carvacrol and rosmarinic acid with Argus lab and ajmalicine, swertiamarin, laminaribiose, catechin with Swissdock found effective against Plasmodium LDH enzyme in our docking study. We found in silico drug docking a better approach to check utility of any chemical as a drug before going through any in vivo or in vitro analysis to shorten out the experiments and cost cutting.


  1. Greenwood B. and Mutabingwa T., Malaria in 2002, Nature.,415, 670672 (2002)
  2. Phillips R.S., Current status of malaria and potential for Control, Clin. Microbiol. Rev., 14(1), 208226 (2001)
  3. Sachs J. and Malaney P., The economic and social burden of Malaria, Nature,415, 680-685 (2002)
  4. Kevin B.J., Chloroquine resistance in Plasmodium vivax, Antimicrob. Agents Chemother.,98(41), 40754083 (2004)
  5. Spudick M.J., Garcia S.L., Graham M.D. and Haake A.D., Diagnostic and therapeutic pitfalls associated with primaquine tolerant Plasmodium vivax, J. Clin. Microbiol.,43(2), 978981 (2005)
  6. Vennerstrom J., Nuzum E., Miller R., Dorn A., Gerena L. et al., 8- Aminoquinolines active against blood stage Plasmodium falciparum in vitro inhibit hematin polymerization, Antimicrob. Agents Chemother., 43, 598602 (1999)
  7. Oliveira-Ferreira J., Lacerda M. V., Brasil P., Ladislau J. L., Tauil P. L. et al., Malaria in Brazil: an overview, Malar. J.,, 115 (2010)
  8. Krettli A., Development of new antimalarials from medicinal Brazilian plants extracts, synthetic molecules and drug combinations, Expert. Opin. Drug Discov., 4(2), 95108 (2009)
  9. Krettli A.U., Adebayo J.O. and Krettli L.G., Testing of natural products and synthetic molecules aiming at new antimalarials, Curr. Drug Targets,10, 261270 (2009)
  10. Das S. K. and Vasudevan D. M., Tulsi: The Indian holy power plant, 5(4), 279-283 (2006)
  11. Katewa S. S. and Arora A., Indian Drugs, 38(1), 6 (2001)
  12. Lang- Unnasch N. and Murphy A. D., Metabolic changes of the malaria parasite during the transition from the human to mosquito host, 52, 561-590 (1998)
  13. Wiwanitkit V., Plasmodium and host LDH molecular function and biological pathways: Implication for antimalarial drug discovery, Chulalongkorn University, Thailand (2007)
  14. Makler M.T. and Hinrichs D.J., Measurement of the lactate dehydrogenase activity of Plasmodium falciparum as an assessment of parasitemia, Am. J. Trop. Med. Hyg., 48, 205-210 (1993)
  15. Dunn C.R., Banfield M.J., Barker J.J., Higham C.W., Moreton K.M., Turgut-Balik D., Brady R.L. and Holbrook J.J., The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for antimalarial design, Nature Struct. Biol.; , 912915 (1996)
  16. Prakash N., Patel S., Faldu N., Ranjan R. and Sudheer D.V.N., Molecular docking studies of antimalarial drugs for malaria, J. Comput .Sci. Syst. Biol., 3(3), 70-73 (2010)
  17. Thompson M.A., Molecular docking using Argus Lab, an efficient shape based search algorithm and the A Score scoring function ACS meeting, Philadelphia, 172, CINF 42, PA (2004)
  18. Grosdidier A., Zoete V. and Michielin O., SwissDock, a protein-small molecule docking web service based on EADock DSS, Nucleic Acid Research,(2011)
  24. (2012)