Screening natural products database for identification of potential antileishmanial chemotherapeutic agents

Interdisciplinary Sciences – Computational Life Sciences

Volumn 3, Issue 3, 2011, Pages 217-231

  Venkatesan, Santhosh K ^a   Saudagar, Prakash ^a   Shukla, Anil K ^a   Dubey, Vikash Kumar ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

leishmaniasis; ligand clustering; natural product; therapeutics; virtual screening

Indexed keywords

KINETOPLASTIDA; LEISHMANIA DONOVANI; LEISHMANIA INFANTUM; PROTOZOA; TRYPANOSOMATIDAE;

ANTIPROTOZOAL AGENT; BIOLOGICAL PRODUCT; LIGAND;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DATA BASE; DRUG EFFECT; DRUG SCREENING; ENZYME ACTIVE SITE; LEISHMANIA; METHODOLOGY;

ANTIPROTOZOAL AGENTS; BIOLOGICAL AGENTS; CATALYTIC DOMAIN; DATABASES AS TOPIC; DRUG EVALUATION, PRECLINICAL; LEISHMANIA; LIGANDS; MODELS, MOLECULAR;

EID: 80755142191     PISSN: 19132751     EISSN: 18671462     Source Type: Journal    
DOI: 10.1007/s12539-011-0101-x     Document Type: Article

References (21)

1. Baiocco, P., Colotti, G., Franceschini, S., Andrea, I. 2009. Molecular basis of antimony treatment in leishmaniasis. J Med Chem 52, 2603-2612.
2. Bond, C. S., Zhang, Y., Berriman, M., Cunningham, M. L., Fairlamb, A. H., Hunter, A. N. 1999. Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structurebased discovery of new natural product inhibitors. Structure 7, 81-89.
3. Bouvier, G., Evrard-Todeschi, N., Girault, J. P., Bertho, G. 2010. Automatic clustering of docking poses in virtual screening process using self-organising map. Bioinformatics 26, 53-60.
4. Croft, S. L., Sundar, S., Fairlamb A. H. 2006. Drug resistance in leishmaniasis. Clin Microbiol Rev 19, 111-126.
5. Fairlamb, A. H., Blackburn, P., Ulrich, P., Chait, B. T., Cerami, A. 1985. Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 227, 1485-1487.
6. Fairlamb, A. H., Cerami, A. 1992. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 46, 695-729.
7. Holloway, G. A., Charman, W. N., Fairlamb, A. H., Brun, R., Kaiser, M., Kostewicz, E., Novello, P. M., Parisot, J. P., Richardson, J., Street, I. P., Watson, K. G., Baell J. B. 2009. Trypanothione reductase highthroughput screening campaign identifies novel classes of inhibitors with antiparasitic activity. Antimicrob Agents Chemother 53, 2824-2833.
8. Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19, 1639-1662.
9. Murray, H. W., Berman, J. D., Davies, C. R., Saravia, N. G. 2005. Advances in leishmaniasis. Lancet 366, 1561-1577.
10. Newman, D. J., Cragg, G. M. 2007. Natural poducts as sources of new drugs over the last 25 years. J Nat Prod 70, 461-477.
11. Orhan, I., Şener, B., Kaiser, M., Brun, R., Tasdemir, D. 2010. IInhibitory activity of marine sponge-derived natural products against parasitic protozoa. Mar Drugs 8, 47-58.
12. Perez-Pineiro, R., Burgos, A., Jones, D. C., Andrew, L. C., Rodriguez, H., Suarez, M., Fairlamb, A. H., Wishart, D. S. 2009. Development of a novel virtual screening cascade protocol to identify potential trypanothione reductase inhibitors. J Med Chem 52, 1670-1680.
13. Rivarola, H. W., Paglini-Oliva, P. A. 2002. Trypanosoma cruzi trypanothione reductase inhibitors: Phenothiazines and related compounds modify experimental Chagas' disease evolution. Curr Drug Targets Cardiovasc Haematol Disord 2, 43-52.
14. Sanner, M. F. 1999. Python: A programming language for software integration and development. J Mol Graphics Mod 17, 57-61.
15. Shukla, A. K., Singh, B. K., Patra, S., Dubey, V. K. 2010. Rational approaches for drug designing against Leishmaniasis. Appl Biochem Biotechnol 160, 2208-2218.
16. Shukla, A. K., Patra, S., Dubey, V. K. 2011. Evaluation of selected antitumor agents as subversive substrate and potential inhibitor of trypanothione reductase: An alternative approach for chemotherapy of Leishmaniasis. Mol Cell Biochem, DOI: 10. 1007/s11010-011-0762-0.
17. Tovar, J., Cunningham, M. I., Smith, A. C., Croft, S. I., Fairlamb, A. H. 1998. Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: Effect on parasite intracellular survival. Proc Natl Acad Sci USA 95, 5311-5316.
18. Venkatesan, S. K., Shukla, A. K., Dubey, V. K. 2010. Molecular docking studies of selected tricyclic and quinone derivatives on trypanothione reductase of Leishmania infantum. J Comput Chem 31, 2463-2472.
19. Vogt, A., Tamewitz, A., Skoko, J., Sikorski, R. P., Giuliano, K. A., Lazo, J. S. 2005. The benzo[c]phenanthridine alkaloid, sanguinarine, is a selective, cell-active inhibitor of mitogen-activated protein kinase phosphatase-1. J Biol Chem 280, 19078-19086.
20. Wallace, A. C., Laskowski, R. A., Thornton, J. M. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Prot Eng 8, 127-134.
21. Zhang, Y., Bond, C. S., Bailey, S., Cunningham, M. L., Fairlamb, A. H., Hunter, W. N. 1996. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2. 3 Å resolution. Protein Sci 5, 52-61.