Anti-Trypanosoma cruzi activity of nicotinamide

Acta Tropica

Volumn 122, Issue 2, 2012, Pages 224-229

  Soares, Milena B P ^a,b   Silva, Cinara V ^a   Bastos, Tanira M ^a   Guimarães, Elisalva T ^a   Figueira, Claudio P ^a   Smirlis, Despina ^c   Azevedo, Walter F ^d  

^a INSTITUTO OSWALDO CRUZ   (Brazil)

^b HOSPITAL SÃO RAFAEL   (Brazil)

^c HELLENIC PASTEUR INSTITUTE   (Greece)

^d PONTIFICAL CATHOLIC UNIVERSITY OF RIO GRANDE DO SUL   (Brazil)

Author keywords

Nicotinamide; Sirtuin; Trypanosoma cruzi; Virtual screening

Indexed keywords

NICOTINAMIDE; SIRTUIN 2; TRYPANOSOMA CRUZI SIRTUIN 2; UNCLASSIFIED DRUG;

ANTIPARASITE DEFENSE; CYTOPLASM; DRUG; ENZYME ACTIVITY; LIGAND; ORGANIC COMPOUND; PARASITE;

AMASTIGOTE; ANIMAL CELL; ANIMAL TISSUE; ANTIPROTOZOAL ACTIVITY; ARTICLE; CELL ULTRASTRUCTURE; CELL VACUOLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG SCREENING; EPIMASTIGOTE; GROWTH INHIBITION; HUMAN; IC 50; IN VITRO STUDY; MICROBIAL GROWTH; MICROBIAL VIABILITY; MITOCHONDRION; MOLECULAR DOCKING; MOUSE; NONHUMAN; PERITONEUM MACROPHAGE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; TRYPANOSOMA CRUZI; TRYPOMASTIGOTE;

AMINO ACID SEQUENCE; CELL SURVIVAL; CHAGAS DISEASE; DRUG DISCOVERY; HUMANS; LIGANDS; MACROPHAGES; MODELS, MOLECULAR; NIACINAMIDE; PROTOZOAN PROTEINS; SEQUENCE ALIGNMENT; SIRTUINS; TRYPANOCIDAL AGENTS; TRYPANOSOMA CRUZI;

TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI; TRYPANOSOMATIDAE;

EID: 84857740405     PISSN: 0001706X     EISSN: 18736254     Source Type: Journal    
DOI: 10.1016/j.actatropica.2012.01.001     Document Type: Article

References (36)

1. Alsford S., Kawahara T., Isamah C., Horn D. A sirtuin in the African trypanosome is involved in both DNA repair and telomeric gene silencing but is not required for antigenic variation. Mol. Microbiol. 2007, 63:724-736.
2. Denu J.M. Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases. Trends Biochem. Sci. 2003, 28:41-48.
3. Denu J.M. Vitamin B3 and sirtuin function. Trends Biochem. Sci. 2005, 30:479-483.
4. Flodin N.W. Niacin and niacinamide. Curr. Top. Nutr. Dis. 1988, 20:129-138.
5. García-Salcedo J.A., Gijón P., Nolan D.P., Tebabi P., Pays E. A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei. EMBO J. 2003, 22:5851-5862.
6. Gazanion E., Vergnes B., Seveno M., Garcia D., Oury B., Ait-Oudhia K., Ouaissi A., Sereno D. In vitro activity of nicotinamide/antileishmanial drug combinations. Parasitol. Int. 2011, 60:19-24.
7. Hoff K.G., Avalos J.L., Sens K., Wolberger C. Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure 2006, 14:1231-1240.
8. Irwin J.J., Shoichet B.K. ZINC-a free database of commercially available compounds for virtual screening. J. Chem. Inf. Model. 2005, 45:177-182.
9. Jackson M.D., Schmidt M.T., Oppenheimer N.J., Denu J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 2003, 278:50985-50998.
10. Jeanguenin L., Lara-Núñez A., Rodionov D.A., Osterman A.L., Komarova N.Y., Rentsch D., Gregory J.F., Hanson A.D. Comparative genomics and functional analysis of the NiaP family uncover nicotinate transporters from bacteria, plants, and mammals. Funct. Integr. Genomics 2011, Sep 28, 2011 (Epub ahead of print).
11. Kadam R.U., Kiran V.M., Roy N. Comparative protein modeling and surface analysis of Leishmania sirtuin: a potential target for antileishmanial drug discovery. Bioorg. Med. Chem. Lett. 2006, 16:6013-6018.
12. Kadam R.U., Tavares J., Kiran V.M., Cordeiro A., Ouaissi A., Roy N. Structure function analysis of Leishmania sirtuin: an ensemble of in silico and biochemical studies. Chem. Biol. Drug Des. 2008, 71:501-506.
13. Kaur S., Shivange A.V., Roy N. Structural analysis of trypanosomal sirtuin: an insight for selective drug design. Mol. Divers. 2010, 14:169-178.
14. Kowieski T.M., Lee S., Denu J.M. Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2. J. Biol. Chem. 2008, 283:5317-5326.
15. Leroux A.E., Maugeri D.A., Cazzulo J.J., Nowicki C. Functional characterization of NADP-dependent isocitrate dehydrogenase isozymes from Trypanosoma cruzi. Mol. Biochem. Parasitol. 2011, 177:61-64.
16. Lipinski C.A., Lombardo F., Dominy B.W., Feeney P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 1997, 23:3-26.
17. Moreira D.R., Leite A.C., dos Santos R.R., Soares M.B. Approaches for the development of new anti-Trypanosoma cruzi agents. Curr. Drug Targets 2009, 10:212-231.
18. Nguewa P.A., Fuertes M.A., Valladares B., Alonso C., Pérez J.M. Programmed cell death in trypanosomatids: a way to maximize their biological fitness. Trends Parasitol. 2004, 20:375-380.
19. Oprea T.I., Davis A.M., Teague S.J., Leeson P.D. Is there a difference between leads and drugs a historical perspective. J. Chem. Inf. Comput. Sci. 2001, 41:1308-1315.
20. Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
21. Prusty D., Mehra P., Srivastava S., Shivange A.V., Gupta A., Roy N., Dhar S.K. Nicotinamide inhibits Plasmodium falciparum Sir2 activity in vitro and parasite growth. Microbiol. Lett. 2008, 282:266-272.
22. Sauve A.A., Celic I., Avalos J., Deng H., Boeke J.D., Schramm V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 2001, 40:15456-15463.
23. Sauve A.A., Schramm V.L. SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates. Curr. Med. Chem. 2004, 11:807-826.
24. Schmidt M.T., Smith B.C., Jackson M.D., Denu J.M. Co-enzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J. Biol. Chem. 2004, 279:40122-40129.
25. Schuetz A., Min J., Antoshenko T., Wang C.L., Allali-Hassani A., Dong A., Loppnau P., Vedadi M., Bochkarev A., Sternglanz R., Plotnikov A.N. Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin. Structure 2007, 15:377-389.
26. Sereno D., Monte Alegre A., Silvestre R., Vergnes B., Ouaissi A. In vitro antileishmanial activity of nicotinamide. Antimicrob. Agents Chemother. 2005, 49:808-812.
27. Soares M.B., Pontes-de-Carvalho L., Ribeiro-dos-Santos R. The pathogenesis of Chagas' disease: when autoimmune and parasite-specific immune responses meet. An. Acad. Bras. Cienc. 2001, 73:547-559.
28. Sofue M., Yoshimura Y., Nishida M., Kawada J. Possible multifunction of glucose transporter. Transport of nicotinamide by reconstituted liposomes. Biochem. J. 1992, 288:669-674.
29. Szczepankiewicz B.G., Ng P.Y. Sirtuin modulators: targets for metabolic diseases and beyond. Curr. Top. Med. Chem. 2008, 8:1533-1544.
30. Taunton J., Hassig C.A., Schreiber S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 1996, 272:408-411.
31. Thomsen R., Christensen M.H. MolDock: a new technique for high-accuracy molecular docking. J. Med. Chem. 2006, 49:3315-3321.
32. Timmers L.F.S., Pauli I., Caceres R.A., De Azevedo W.F. Drug-binding databases. Curr. Drug Targets 2008, 9:1092-1099.
33. Uchoa H.B., Jorge G.E., Da Silveira N.J.F., Camera J.C., Canduri F., De Azevedo W.F. Parmodel: a web server for automated comparative modeling of proteins. Biochem. Biophys. Res. Commun. 2004, 325:1481-1486.
34. Veber D.F., Johnson S.R., Cheng H.Y., Smith B.R., Ward K.W., Kopple K.D. Molecular properties that influence the oral bioavailability of drug candidates. J. Med. Chem. 2002, 45:2615-2623.
35. WHO, 2002. Control of Chagas Disease. World Health Organ. Tech. Rep. Ser. 905, pp. 1-109.
36. Zemzoumi K., Sereno D., François C., Guilvard E., Lemesre J.L., Ouaissi A. Leishmania major: cell type dependent distribution of a 43kDa antigen related to silent information regulatory-2 protein family. Biol. Cell 1998, 90:239-245.