Esters of quinoxaline-7-carboxylate-1,4-di-
4-di-N-oxide
quinoxaline 1
trichomoniasis
triosephosphate isomerase inhibitor
Journal
Acta pharmaceutica (Zagreb, Croatia)
ISSN: 1846-9558
Titre abrégé: Acta Pharm
Pays: Poland
ID NLM: 9303678
Informations de publication
Date de publication:
01 Sep 2021
01 Sep 2021
Historique:
accepted:
09
10
2020
entrez:
19
1
2023
pubmed:
31
12
2020
medline:
31
12
2020
Statut:
epublish
Résumé
Trichomoniasis is a public health problem worldwide. Trichomoniasis treatment consists of the use of nitroimidazole derivatives; however, therapeutic ineffectiveness occurs in 5 to 20 % of the cases. Therefore, it is essential to propose new pharmacological agents against this disease. In this work, esters of quinoxaline-7-carboxylate-1,4-di-
Identifiants
pubmed: 36654088
pii: acph-2021-0032
doi: 10.2478/acph-2021-0032
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
485-495Informations de copyright
© 2021 Isidro Palos et al., published by Sciendo.
Références
1. D. Leitsch, Drug resistance in the microaerophilic parasite Giardia lamblia, Curr. Trop. Med. Rep.2 (2015) 128–135; https://doi.org/10.1007/s40475-015-0051-110.1007/s40475-015-0051-1452369426258002
2. B. R. Ansell, M. J. McConville, S. Y. Ma’ayeh, M. J. Dagley, R. B. Gasser, S. G. Svärd and A. R. Jex, Drug resistance in Giardia duodenalis, Biotechnol. Adv.33 (2015) 888–901; https://doi.org/10.1016/j.biotechadv.2015.04.00910.1016/j.biotechadv.2015.04.00925922317
3. C. B. Menezes, A. P. Frasson and T. Tasca, Trichomoniasis – are we giving the deserved attention to the most common non-viral sexually transmitted disease worldwide?, Microb. Cell3 (2016) 404–419; https://doi.org/10.15698/mic2016.09.52610.15698/mic2016.09.526535456828357378
4. D. Leitsch, Recent advances in the Trichomonas vaginalis field, F1000Res.5 (2016) Article ID 162 (7 pages); https://doi.org/10.12688/f1000research.7594.110.12688/f1000research.7594.1475539626918168
5. P. Kissinger, Trichomonas vaginalis: a review of epidemiologic, clinical and treatment issues, BMC Infect. Dis.15 (2015) Article ID 307 (8 pages); https://doi.org/10.1186/s12879-015-1055-010.1186/s12879-015-1055-0452574926242185
6. P. Upcroft and J. A. Upcroft, Drug targets and mechanisms of resistance in the anaerobic protozoa, Clin. Microbiol. Rev.14 (2001) 150–164; https://doi.org/10.1128/CMR.14.1.150-164.200110.1128/CMR.14.1.150-164.20018896711148007
7. P. A. Cano, A. Islas-Jácome, J. González-Marrero, L. Yépez-Mulia, F. Calzada and R. Gámez-Montaño, Synthesis of 3-tetrazolylmethyl-4H-chromen-4-ones via Ugi-azide and biological evaluation against Entamoeba histolytica, Giardia lamblia and Trichomona vaginalis, Bioorg. Med. Chem.22 (2014) 1370–1376; https://doi.org/10.1016/j.bmc.2013.12.06910.1016/j.bmc.2013.12.06924468633
8. S. Chaturvedi, M. Y. Malik, M. Rashid, S. Singh, V. Tiwari, P. Gupta, S. Shukla, S. Singh and M. Wahajuddin, Mechanistic exploration of quercetin against metronidazole induced neurotoxicity in rats: possible role of nitric oxide isoforms and inflammatory cytokines, Neurotoxicology79 (2020) 1–10; https://doi.org/10.1016/j.neuro.2020.03.00210.1016/j.neuro.2020.03.00232151614
9. J. Jampilek, Recent advances in design of potential quinoxaline anti-infectives, Curr. Med. Chem.21 (2014) 4347–4373; https://doi.org/10.2174/092986732166614101119482510.2174/092986732166614101119482525312209
10. I. Balderas-Renteria, P. Gonzalez-Barranco, A. Garcia, B. K. Banik and G. Rivera, Anticancer drug design using scaffolds of β-lactams, sulfonamides, quinoline, quinoxaline and natural products. Drugs advances in clinical trials, Curr. Med. Chem.19 (2012) 4377–4398; https://doi.org/10.2174/09298671280325159310.2174/09298671280325159322709002
11. N. B. Patel, J. N. Patel, A. C. Purohit, V. M. Patel, D. P. Rajani, R. Moo-Puc, J. C. Lopez-Cedillo, B. Nogueda-Torres and G. Rivera, In vitro and in vivo assessment of newer quinoxaline-oxadiazole hybrids as antimicrobial and antiprotozoal agents, Int. J. Antimicrob. Agents50 (2017) 413–418; https://doi.org/10.1016/j.ijantimicag.2017.04.01610.1016/j.ijantimicag.2017.04.01628687457
12. G. Cheng, W. Sa, C. Cao, L. Guo, H. Hao, Z. Liu, X. Wang and Z. Yuan, Quinoxaline 1,4-di-N-oxides: Biological activities and mechanisms of actions, Front. Pharmacol.7 (2016) Article ID 64 (21 pages); https://doi.org/10.3389/fphar.2016.0006410.3389/fphar.2016.00064480018627047380
13. R. El Aissi, J. Liu, S. Besse, D. Canitrot, O. Chavignon, J. M. Chezal, E. Miot-Noirault and E. Moreau, Synthesis and biological evaluation of new quinoxaline derivatives of ICF01012 as melanoma-targeting probes, ACS Med. Chem. Lett.5 (2014) 468–473; https://doi.org/10.1021/ml400468x10.1021/ml400468x402760924900863
14. J. C. Villalobos-Rocha, L. Sánchez-Torres, B. Nogueda-Torres, A. Segura-Cabrera, C. A. García-Pérez, V. Bocanegra-García, I. Palos, A. Monge and G. Rivera, Anti-Trypanosoma cruzi and anti-leishmanial activity by quinoxaline-7-carboxylate 1,4-di-N-oxide derivatives, Parasitol. Res.113 (2014) 2027–2035; https://doi.org/10.1007/s00436-014-3850-810.1007/s00436-014-3850-824691716
15. K. F. Chacón-Vargas, S. Andrade-Ochoa, B. Nogueda-Torres, D. C. Juárez-Ramírez, E. E. Lara-Ramírez, R. Mondragón-Flores, A. Monge and G. Rivera, L. E. Sánchez-Torres, Isopropyl quinoxaline-7-carboxylate 1,4-di-N-oxide derivatives induce regulated necrosis-like cell death on Leish-mania (Leishmania) mexicana, Parasitol. Res.117 (2018) 45–58; https://doi.org/10.1007/s00436-017-5635-310.1007/s00436-017-5635-329159705
16. M. Quiliano, A. Pabón, G. Ramirez-Calderon, C. Barea, E. Deharo, S. Galiano and I. Aldana, New hydrazine and hydrazide quinoxaline 1,4-di-N-oxide derivatives: In silico ADMET, antiplasmo-dial and antileishmanial activity. Bioorg. Med. Chem. Lett.27 (2017) 1820–1825; https://doi.org/10.1016/j.bmcl.2017.02.04910.1016/j.bmcl.2017.02.04928291694
17. B. E. Duque-Montaño, L. C. Gómez-Caro, M. Sanchez-Sanchez, A. Monge, E. Hernández-Baltazar, G. Rivera and O. Torres-Angeles, Synthesis and in vitro evaluation of new ethyl and methyl quinoxaline-7-carboxylate 1,4-di-N-oxide against Entamoeba histolytica, Bioorg. Med. Chem.21 (2013) 4550–4558; https://doi.org/10.1016/j.bmc.2013.05.03610.1016/j.bmc.2013.05.03623787289
18. L. C. Gómez-Caro, M. Sánchez-Sánchez, V. Bocanegra-García, A. Monge and G. Rivera, Synthesis of quinoxaline 1,4-di-N-oxide derivatives on solid support using room temperature and microwave-assisted solvent-free procedures, Quim. Nova34 (2011) 1147–1151; https://doi.org/10.1590/S0100-4042201100070000810.1590/S0100-40422011000700008
19. E. Hernández-Núñez, H. Tlahuext, R. Moo-Puc, H. Torres-Gómez, R. Reyes-Martínez, R Cedillo-Rivera, C. Nava-Zuazo and G. Navarrete-Vazquez, Synthesis and in vitro trichomonicidal, giardicidal and amebicidal activity of N-acetamide(sulfonamide)-2-methyl-4-nitro-1H-imidazoles, Eur. J. Med. Chem.44 (2009) 2975–2984; https://doi.org/10.1016/j.ejmech.2009.01.00510.1016/j.ejmech.2009.01.00519208443
20. B. R. Brooks, C. L. Brooks, A. D. Mackerell, L. Nilsson, R. J. Petrella, B. Roux, Y. Won, G. Archontis, C. Bartels, S. Boresch, A. Caflisch, L. Caves, Q. Cui, A. R. Dinner, M. Feig, S. Fischer, J. Gao, M. Hodoscek, W. Im, K. Kuczera, T. Lazaridis, J. Ma, V. Ovchinnikov, E. Paci, R. W. Pastor, C. B. Post, J. Z. Pu, M. Schaefer, B. Tidor, R. M. Venable, H. L. Woodcock, X. Wu, W. Yang, D. M. York and M. Karplus, CHARMM: The biomolecular simulation program, J. Comput. Chem.30 (2009) 1545–1614; https://doi.org/10.1002/jcc.2128710.1002/jcc.21287281066119444816
21. P. R. Gerber and K. Müller, MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry, J. Comput. Aided Mol. Des.9 (1995) 251–268; https://doi.org/10.1007/bf0012445610.1007/BF00124456
22. C. A. Del Carpio, Y. Takahashi and S.-i. Sasaki, A new approach to the automatic identification of candidates for ligand receptor sites in proteins: (I) Search for pocket regions, J. Mol. Graph.11 (1993) 23–29; https://doi.org/10.1016/0263-7855(93)85003-9
23. A. Miranker and M. Karplus, Functionality maps of binding sites: A multiple copy simultaneous search method, Proteins: Struct. Funct. Genet.11 (1991) 29–34; https://doi.org/10.1002/prot.34011010
24. S. Thangapandian, S. John, Y. Lee, S. Kim and K. W. Lee, Dynamic structure-based pharmacophore model development: A new and effective addition in the histone deacetylase 8 (HDAC8) inhibitor discovery, Int. J. Mol. Sci.12 (2011) 9440–9462; https://doi.org/10.3390/ijms1212944010.3390/ijms12129440
25. A. Wadood, M. Ghufran, S. F. Hassan, H. Khan, S. S. Azam and U. Rashid, In silico identification of promiscuous scaffolds as potential inhibitors of 1-deoxy-D-xylulose 5-phosphate reductoisom-erase for treatment of Falciparum malaria, Pharm. Biol.55 (2017) 19–32; https://doi.org/10.1080/13880209.2016.122577810.1080/13880209.2016.1225778
26. A. M. Clark and P. Labute, 2D depiction of protein–ligand complexes, J. Chem. Inf. Model. 47 (2007) 1933–1944; https://doi.org/10.1021/ci700147310.1021/ci7001473
27. S. Lara-González, P. Estrella, C. Portillo, M. E. Cruces, P. Jiménez-Sandoval, J. Fattori, A. C. Migliorini-Figueira, M. López-Hidalgo, C. Díaz-Quezada, M. López-Castillo, C. H. Trasviña-Arenas, E. Sánchez-Sandoval, A. Gómez-Puyou, J. Ortega-López, R. Arroyo, C. G. Benítez-Cardoza and L. G. Brieba, Substrate-induced dimerization of engineered monomeric variants of triosephosphate isomerase from Trichomonas vaginalis, PLoS ONE10 (2015) e0141747; https://doi.org/10.1371/journal.pone.014174710.1371/journal.pone.0141747
28. P. Jiménez-Sandoval, J. L. Vique-Sanchez, M. L. Hidalgo, G. Velazquez-Juarez, C. Díaz-Quezada, L. F. Arroyo-Navarro, G. M. Morán, J. Fattori, A. J. Diaz-Salazar, E. Rudiño-Pinera, R. Sotelo-Mundo, A. C. Migliorini-Figueira, S. Lara-Gonzalez, C. G. Benítez-Cardoza and L. G. Brieba, A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase, Biochim. Biophys. Acta – Prot. Proteom.1865 (2017) 1423–1432; https://doi.org/10.1016/j.bbapap.2017.07.01410.1016/j.bbapap.2017.07.014
29. G. Álvarez, J. Martínez, B. Aguirre-López, N. Cabrera, L. Pérez-Díaz, M. T. de Gómez-Puyou, A. Gómez-Puyou, R. Pérez-Montfort, B. Garat, A. Merlino, M. González and H. Cerecetto, New chemotypes as Trypanosoma cruzi triosephosphate isomerase inhibitors: a deeper insight into the mechanism of inhibition, J. Enzyme Inhib. Med. Chem.29 (2014) 198–204; https://doi.org/10.3109/14756366.2013.76541510.3109/14756366.2013.765415
30. A. Gómez-Puyou, E. Saavedra-Lira, I. Becker, R. A. Zubillaga, A. Rojo-Dominguez and R. Perez-Montfort, Using evolutionary changes to achieve species-specific inhibition of enzyme action — studies with triosephosphate isomerase, Chem. Biol.2 (1995) 847–855; https://doi.org/10.1016/1074-5521(95)90091-810.1016/1074-5521(95)90091-8
31. M. de N. C. Soeiro and S. L. Castro, Screening of potential anti-Trypanosoma cruzi candidates: In vitro and in vivo studies, Open Med. Chem. J.5 (2011) 21–30; https://doi.org/10.2174/187410450110501002110.2174/1874104501105010021310389721629508
32. G. Álvarez, B. Aguirre-López, J. Varela, M. Cabrera, A. Merlino, G. V. López, M. L. Lavaggi, W. Porcal, R. Di Maio, M. González, H. Cerecetto, N. Cabrera, R. Pérez-Montfort, M. Tuena de Gómez-Puyou and A. Gómez-Puyou, Massive screening yields novel and selective Trypanosoma cruzi triosephosphate isomerase dimer-interface-irreversible inhibitors with anti-trypanosomal activity, Eur. J. Med. Chem.45 (2010) 5767–5772; https://doi.org/10.1016/j.ejmech.2010.09.03410.1016/j.ejmech.2010.09.03420889239
33. C. G. Benítez-Cardoza, D. A. Fernández-Velasco and J. L. Vique-Sánchez, Triosephosphate isom-erase inhibitors as potential drugs against Clostridium perfringens, Chem. Sel.5 (2020) 2365–2370; https://doi.org/10.1002/slct.20190463210.1002/slct.201904632
34. J. L. Vique-Sánchez, L. A. Caro-Gómez, L. G. Brieba and C. G. Benítez-Cardoza, Developing a new drug against trichomoniasis, new inhibitory compounds of the protein triosephosphate isomerase, Parasitol. Int.76 (2020) Article ID 102086; https://doi.org/10.1016/j.parint.2020.10208610.1016/j.parint.2020.102086
35. A. Téllez-Valencia, S. Avila-Ríos, R. Pérez-Montfort, A. Rodríguez-Romero, M. Tuena de Gómez-Puyou, F. López-Calahorra and A. Gómez-Puyou, Highly specific inactivation of triosephosphate isomerase from Trypanosoma cruzi, Biochem. Biophys. Res. Commun.295 (2002) 958–963; https://doi.org/10.1016/s0006-291x(02)00796-910.1016/S0006-291X(02)00796-9
36. B. Hernández-Ochoa, G. Navarrete-Vázquez, C. Nava-Zuazo, A. Castillo-Villanueva, S. T. Méndez, A. Torres-Arroyo, S. Gómez-Manzo, J. Marcial-Quino, M. Ponce-Macotela, Y. Rufino-González, M. Martínez-Gordillo, G. Palencia-Hernández, N. Esturau-Escofet, E. Calderon-Jaimes, J. Oria-Hernández and H. Reyes-Vivas, Novel giardicidal compounds bearing proton pump inhibitor scaffold proceeding through triosephosphate isomerase inactivation, Sci. Rep.7 (2017) Article ID 7810; https://doi.org/10.1038/s41598-017-07612-y10.1038/s41598-017-07612-y555269128798383