Protein-ligand interaction studies on 2, 4, 6-trisubstituted triazine derivatives as anti-malarial DHFR agents using AutoDock

Research Journal of Biotechnology

Volumn 3, Issue 3, 2008, Pages 18-23

  Pavani, P ^c   SarvaMangala D , ^c   Murthy, J V V S ^a   Babu, Ajay P ^b  

^a Department of Biotechnology   (India)

^b Research Centre   (India)

^c NONE

Author keywords

Anti malarial DHFR agents; AutoDock; Protein ligand interaction; Substituted triazine

Indexed keywords

PLASMODIUM FALCIPARUM; RUMEX;

EID: 77949511949     PISSN: 09736263     EISSN: None     Source Type: Trade Journal    
DOI: None     Document Type: Article

References (20)

1. Dan McElheny., Jason R., Schnell., Jonathan C., Lansing H., Jane Dyson and Peter E., Wright Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis, Proc Natl Acad Sci, U S A., 102, 5032 (2005)
2. Nicotine G., Ribonucleotide reductase inhibitors: new strategies for cancer chemotherapy, Critical Reviews in oncology/Hematology, 22, 89 (1996)
3. Trujillo M., Duncan R. and Santi D. V., Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme, Protein Eng, 10, 567 (1997)
4. Hillcoat B. L. and Blakely R. L., Dihydrofolate Reductase of Streptococcus faecalis I. Purification and some properties of Reductase from the wild strain and from strain A, J. Biol. Chem., 241, 2995 (1966)
5. Hitchings G. H., Part II. Pyrimethamine: The use of an antimetabolite in the chemotherapy of malaria and other infections, Clin. Pharmacol. Ther, 1, 570 (1960)
6. Houghton P. J., Germain G. S., Hazelton B. J., Pennington J. W. and Houghton J. A., Mutants of human colon adenocarcinoma, selected for thymidylate synthase deficiency, Proc. Natl. Acad. Sci, U. S. A., 86, 1377 (1989)
7. Yoshioka A., Tanaka S., Hiraoka O., Koyama Y., Hirota Y., Ayusawa D., Seno T., Garrett C. and Wataya Y., Deoxyribonucleoside triphosphate imbalance. 5-Fluorodeoxyuridineinduced DNA double strand breaks in mouse FM3A cells and the mechanism of cell death, J. Biol. Chem., 262, 8235 (1987)
8. Foote S. J., Galatis D. and Cowman A. F., Amino acids in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum involved in cycloguanil resistance differ from those involved in pyrimethamine resistance, Proc. Natl. Acad. Sci, U. S. A., 87, 3014 (1990)
9. Nzila-Mounda A., Mberu E. K., Sibley C. H., Plowe, C. V., Winstanley P. A. and Watkins W. M., Kenyan Plasmodium falciparum Field Isolates: Correlation between Pyrimethamine and Chlorcycloguanil Activity In Vitro and Point Mutations in the Dihydrofolate Reductase Domain, Antimicrob. Agents Chemotherapy, American Society for Microbiology, 42, 164 (1998)
10. Canfield C. J., Milhous W. K., Ager A. L., Rossan R. N., Sweeney T. R., Lewis N. J. and Jacobus D. P., a Potent, Orally Active Antimalarial from a New Class of Folic Acid Antagonists, Am. J. Trop. Med. Hyg., 49, 121 (1993)
11. Rathod P. K., and Reshmi S., Essential Protein-Protein Interactions between Plasmodium falciparum Thymidylate Synthase and Dihydrofolate Reductase Domains, Antimicrob. Agents Chemothearapy, J Biol Chem., 38(3), 476 (1994)
12. Jay F Davies II., Tavner J., Delcamp Neal J., Prendergad Victor A., Ashford James., Freisheim H. and Joseph Kraut., Crystal Structures of Recombinant Human Dihydrofolate Reductase Complexed with Folate and 5-Deazafolatet, Biochemistry, 29, 9467 (1990)
13. Yuthavong Y., Yuvaniyama J., Chitnumsum P., Vanichtanankul J., Chusacultanachai S., Tarnchompoo T., Vilaivan B. and Kamchonwong S., Malarial (Plasmodium falciparum) dihydrofolate reductase-thymidylate synthase: structural basis for antifolate resistance and development of effective inhibitors, Parasitology, 130, 249 (2005)
14. Morris G. M., Goodsell D. S., Halliday R. S., Huey R., Hart W. E., Belew R. K. and Olson A. J., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, J. Comput Chem, 19, 1639 (1998)
15. Kongsaeree P., Khongsuk P., Leartsakulpanich U., Chitnumsub P., Tarnchompoo B., Walkinshaw M. D. and Yuthavong Y., Crystal structure of dihydrofolate reductase from Plasmodium vivax: pyrimethamine displacement linked with mutation-induced resistance, Proc. Natl. Acad. Sci. U. S. A., 102, 13046 (2005)
16. Berman H. M., Westbrook J., Feng Z., Gilliland G., Bhat T. N., H. Weissig H., Shindyalov I. N. and Bourne P. E., The Protein Data Bank., Nucleic Acids Research, 28, 235 (2000)
17. Weiner S. J., Kollman P. A., Case D. A., Singh U. C., Ghio C., Alagona G., Profeta S. and Weine P., A new force field for molecular mechanical simulation of nucleic acids and proteins, J. Am. Chem. Soc., 106, 765 (1984)
18. Gasteiger J. and Marsalis M., Iterative Partial Equalization of Orbital Electro negativity-A Rapid Access to Atomic Charges, Tetrahedron, 36, 3219 (1980)
19. Mehler E. L. and Solmajer T., Electrostatic effects in proteins: Comparison of dielectric and charge models, Protein Eng., 4, 903 (1991)
20. Richardson C. M., Nunns C. L., Williamson D. S., Parratt M. J., Dokurno P., Howes R., Borgognoni J., Drysdale M. J., Finch H., Hubbard R. E., Jackson P. S., Kierstan P., Lentzen G., Moore J. D., Murray J. B., Simmonite H., Surgenor A. E. and Torrance C. J., Discovery of a Potent Cdk2 Inhibitor with a Novel Binding Mode Using Virtual Screening and Initial, Structure-Guided Lead Scoping, Bioorg. Med. Chem. Lett., 17, 3880 (2007).