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Journal articles on the topic 'Trypanothion reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Tchokouaha Yamthe, Lauve Rachel, Trudy Janice Philips, Dorcas Osei-Safo, et al. "Antileishmanial effects of Sargassum vulgare products and prediction of trypanothione reductase inhibition by fucosterol." Future Drug Discovery 2, no. 3 (2020): FDD41. http://dx.doi.org/10.4155/fdd-2020-0002.

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Aim: To investigate the antileishmanial potency of Sargassum vulgare C. Agardh-derived products and the in silico inhibition of trypanothione reductase by fucosterol. Materials & methods: Sargassum vulgare crude extract and its derived fractions, subfractions and fucosterol were screened against Leishmania major and Leishmania donovani using the MTS and trypanothione reductase colorimetric assays. Macrophages viability was evaluated using the resazurin assay. The inhibition of trypanothione reductase by fucosterol was predicted in silico. Results: The crude extract, fractions 2, 4 and 7, subfractions 8.2 and 8.3 and fucosterol-exhibited antileishmanial activity on promastigote (IC50 = 18.99–156.02 μg/ml), while fraction 1, subfraction 8.2 and fucosterol were active on L. major and L. donovani amastigote (IC50 = 18.47–65.34 μg/ml) with low cytotoxicity. Interestingly, fucosterol showed the best activity against both parasites (IC50 = 18.47–58.21 μg/ml). Strong binding affinities were recorded between fucosterol and Leishmania spp. trypanothione reductases. Conclusion: Fucosterol, which was abundant in S. vulgare, might be responsible for the antileishmanial activity.

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2

Ribeiro, Frederico F., Francisco J. B. M. Junior, Marcelo S. da Silva, Marcus Tullius Scotti, and Luciana Scotti. "Computational and Investigative Study of Flavonoids Active against Trypanosoma cruzi and Leishmania spp." Natural Product Communications 10, no. 6 (2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000630.

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Flavonoid compounds active against Trypanosoma cruzi and Leishmania species were submitted to several methodologies in silico: docking with the enzymes cruzain and trypanothione reductase (from T. cruzi), and N-myristoyltransferase, dihydroorotate dehydrogenase, and trypanothiona reductase (from Leishmania spp). Molecular maps of the complexes and the ligands were calculated. In order to compare and evaluate the antioxidant activity of the flavonoids with their antiprotozoal activity, quantum parameters were calculated. Considering the energies, interactions, and hydrophobic surfaces calculated, the flavonoids chrysin dimethyl ether against T. cruzi, and ladanein against Leishmania sp. presented the best results. The antioxidant activity did not show any correlation with anti-parasitic activity; only chrysin and its dimethyl ether showed favorable anti-parasitic results. This study hopes to contribute to existing research on these natural products against these tropical parasites.

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3

MURGOLO, NICHOLAS J., ANTHONY CERAMI, and GRAEME B. HENDERSON. "Trypanothione Reductase." Annals of the New York Academy of Sciences 569, no. 1 Biomedical Sc (1989): 193–200. http://dx.doi.org/10.1111/j.1749-6632.1989.tb27369.x.

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4

Benson, T. J., J. H. McKie, J. Garforth, A. Borges, A. H. Fairlamb, and K. T. Douglas. "Rationally designed selective inhibitors of trypanothione reductase. Phenothiazines and related tricyclics as lead structures." Biochemical Journal 286, no. 1 (1992): 9–11. http://dx.doi.org/10.1042/bj2860009.

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Trypanothione reductase, an essential component of the anti-oxidant defences of parasitic trypanosomes and Leishmania, differs markedly from the equivalent host enzyme, glutathione reductase, in the binding site for the disulphide substrate. Molecular modelling of this region suggested that certain tricyclic compounds might bind selectively to trypanothione reductase without inhibiting host glutathione reductase. This was confirmed by testing 30 phenothiazine and tricyclic antidepressants, of which clomipramine was found to be the most potent, with a K(i) of 6 microM, competitive with respect to trypanothione. Many of these compounds have been noted previously to have anti-trypanosomal and anti-leishmanial activity and thus they can serve as lead structures for rational drug design.

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5

Marsh, Ian R., and Mark Bradley. "Substrate Specificity of Trypanothione Reductase." European Journal of Biochemistry 243, no. 3 (1997): 690–94. http://dx.doi.org/10.1111/j.1432-1033.1997.00690.x.

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6

Hunter, William N., Susan Bailey, Jarjis Habash, et al. "Active site of trypanothione reductase." Journal of Molecular Biology 227, no. 1 (1992): 322–33. http://dx.doi.org/10.1016/0022-2836(92)90701-k.

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7

Smith, K., A. Borges, M. R. Ariyanayagam, and A. H. Fairlamb. "Glutathionylspermidine metabolism in Escherichia coli." Biochemical Journal 312, no. 2 (1995): 465–69. http://dx.doi.org/10.1042/bj3120465.

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Intracellular levels of glutathione and glutathionylspermidine conjugates have been measured throughout the growth phases of Escherichia coli. Glutathionylspermidine was present in mid-log-phase cells, and under stationary and anaerobic growth conditions accounted for 80% of the total glutathione content. N1,N8-bis(glutathionyl)spermidine (trypanothione) was undetectable under all growth conditions. The catalytic constant kcat/Km of recombinant E. coli glutathione reductase for glutathionylspermidine disulphide was approx. 11,000-fold lower than that for glutathione disulphide. The much higher catalytic constant for the mixed disulphide of glutathione and glutathionylspermidine (11% that of GSSG), suggests a possible explanation for the low turnover of trypanothione disulphide by E. coli glutathione reductase, given the apparent lack of a specific glutathionylspermidine disulphide reductase in E. coli.

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8

Dukhyil, Abdul Aziz A. Bin. "Targeting Trypanothione Reductase of Leishmanial major to Fight Against Cutaneous Leishmaniasis." Infectious Disorders - Drug Targets 19, no. 4 (2019): 388–93. http://dx.doi.org/10.2174/1871526518666180502141849.

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Background: 1.2-2.0 million cases of leishmaniasis occur annually throughout the world. The available drugs like Amphotericin B, antimonials and miltefosine are unable to fulfill the need due to less effectiveness, high toxicity, resistance, high cost and complex route of administration. Leishmania survives inside the macrophages through different evasion mechanisms; one of that is activation of its trypanothione reductase enzyme which neutralizes the reactive oxygen species generated inside the macrophages to kill the parasites. This enzyme is unique and absent in human, therefore in this study I targeted it for screening of new inhibitors to fight against leishmaniasis. Methods: Homology modeling of Leishmania major trypanothione reductase was performed using Phyre2 server. The homology based modelled protein was validated with PROCHECK analysis. Ligplot analysis was performed to predict the active residues inside the binding pocket. Further, virtual screening of ligand library containing 113 ligands from PubChem Bioassay was performed against the target using AutoDock Vina Tool. Results: Top five ligands showed best binding affinity. The molecule having PubChem CID: 10553746 showed highest binding affinity of -11.3 kcal/mol. Over all this molecule showed highest binding affinity and moderate number of hydrogen bonds. Hopefully, this molecule will be able to block the activity of target enzyme, trypanothione reductase of Leishmania major effectively and may work as new molecules to fight against cutaneous leishmanaisis. Conclusion: This study will help the researchers to identify the new molecules which can block the activity of leishmanial-trypanothione reductase, a novel enzyme of trypanosomatids. These screened inhibitors may also be effective not only in leishmaniasis but also other trypanosomatid-mediated infectious diseases.

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9

Zhang, Y., S. Bailey, A. H. Fairlamb, and W. N. Hunter. "Structure of trypanothione reductase fromTrypanosoma cruzi." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (1993): c83. http://dx.doi.org/10.1107/s0108767378097627.

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10

Mezianecherif, D., M. Aumercier, I. Kora, et al. "Trypanosoma cruzi: Immunolocalization of Trypanothione Reductase." Experimental Parasitology 79, no. 4 (1994): 536–41. http://dx.doi.org/10.1006/expr.1994.1114.

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11

Ariyanayagam, Mark R., Sandra L. Oza, Maria Lucia S. Guther, and Alan H. Fairlamb. "Phenotypic analysis of trypanothione synthetase knockdown in the African trypanosome." Biochemical Journal 391, no. 2 (2005): 425–32. http://dx.doi.org/10.1042/bj20050911.

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Trypanothione plays a pivotal role in defence against chemical and oxidant stress, thiol redox homoeostasis, ribonucleotide metabolism and drug resistance in parasitic kinetoplastids. In Trypanosoma brucei, trypanothione is synthesized from glutathione and spermidine by a single enzyme, TryS (trypanothione synthetase), with glutathionylspermidine as an intermediate. To examine the physiological roles of trypanothione, tetracycline-inducible RNA interference was used to reduce expression of TRYS. Following induction, TryS protein was reduced >10-fold and growth rate was reduced 2-fold, with concurrent 5–10-fold decreases in glutathionylspermidine and trypanothione and an up to 14-fold increase in free glutathione content. Polyamine levels were not significantly different from non-induced controls, and neither was the intracellular thiol redox potential, indicating that these factors are not responsible for the growth defect. Compensatory changes in other pathway enzymes were associated with prolonged suppression of TryS: an increase in trypanothione reductase and γ-glutamylcysteine synthetase, and a transient decrease in ornithine decarboxylase. Depleted trypanothione levels were associated with increases in sensitivity to arsenical, antimonial and nitro drugs, implicating trypanothione metabolism in their mode of action. Escape mutants arose after 2 weeks of induction, with all parameters, including growth, returning to normal. Selective inhibitors of TryS are required to fully validate this novel drug target.

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12

Čėnas, Narimantas, Aušra Nemeikaitė-Čėnienė, and Lidija Kosychova. "Single- and Two-Electron Reduction of Nitroaromatic Compounds by Flavoenzymes: Mechanisms and Implications for Cytotoxicity." International Journal of Molecular Sciences 22, no. 16 (2021): 8534. http://dx.doi.org/10.3390/ijms22168534.

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Nitroaromatic compounds (ArNO2) maintain their importance in relation to industrial processes, environmental pollution, and pharmaceutical application. The manifestation of toxicity/therapeutic action of nitroaromatics may involve their single- or two-electron reduction performed by various flavoenzymes and/or their physiological redox partners, metalloproteins. The pivotal and still incompletely resolved questions in this area are the identification and characterization of the specific enzymes that are involved in the bioreduction of ArNO2 and the establishment of their contribution to cytotoxic/therapeutic action of nitroaromatics. This review addresses the following topics: (i) the intrinsic redox properties of ArNO2, in particular, the energetics of their single- and two-electron reduction in aqueous medium; (ii) the mechanisms and structure-activity relationships of reduction in ArNO2 by flavoenzymes of different groups, dehydrogenases-electrontransferases (NADPH:cytochrome P-450 reductase, ferredoxin:NADP(H) oxidoreductase and their analogs), mammalian NAD(P)H:quinone oxidoreductase, bacterial nitroreductases, and disulfide reductases of different origin (glutathione, trypanothione, and thioredoxin reductases, lipoamide dehydrogenase), and (iii) the relationships between the enzymatic reactivity of compounds and their activity in mammalian cells, bacteria, and parasites.

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13

Ondarza, Raúl N., Gerardo Hurtado, Elsa Tamayo, Angélica Iturbe, and Eva Hernández. "Naegleria fowleri: A free-living highly pathogenic amoeba contains trypanothione/trypanothione reductase and glutathione/glutathione reductase systems." Experimental Parasitology 114, no. 3 (2006): 141–46. http://dx.doi.org/10.1016/j.exppara.2006.03.001.

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14

MOUTIEZ, Mireille, Eric QUÉMÉNEUR, Christian SERGHERAERT, Valérie LUCAS, André TARTAR, and Elisabeth DAVIOUD-CHARVET. "Glutathione-dependent activities of Trypanosoma cruzi p52 makes it a new member of the thiol:disulphide oxidoreductase family." Biochemical Journal 322, no. 1 (1997): 43–48. http://dx.doi.org/10.1042/bj3220043.

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Trypanothione:glutathione disulphide thioltransferase of Trypanosoma cruzi (p52) is a key enzyme in the regulation of the intracellular thiolŐdisulphide redox balance by reducing glutathione disulphide. Here we show that p52, like other disulphide oxidoreductases possessing the CXXC active site motif, catalyses the reduction of low-molecular-mass disulphides (hydroxyethyldisulphide) as well as protein disulphides (insulin). However, p52 seems to be a poor oxidase under physiological conditions as evidenced by its very low rate for oxidative renaturation of reduced ribonuclease A. Like thioltransferase and protein disulphide isomerase, p52 was found to possess a glutathione-dependent dehydroascorbate reductase activity. The kinetic parameters were in the same range as those determined for mammalian dehydroascorbate reductases. A catalytic mechanism taking into account both trypanothione- and glutathione-dependent reduction reactions was proposed. This newly characterized enzyme is specific for the parasite and provides a new target for specific chemotherapy.

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15

Lu, Jun, Suman K. Vodnala, Anna-Lena Gustavsson, et al. "Ebsulfur Is a Benzisothiazolone Cytocidal Inhibitor Targeting the Trypanothione Reductase of Trypanosoma brucei." Journal of Biological Chemistry 288, no. 38 (2013): 27456–68. http://dx.doi.org/10.1074/jbc.m113.495101.

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Trypanosoma brucei is the causing agent of African trypanosomiasis. These parasites possess a unique thiol redox system required for DNA synthesis and defense against oxidative stress. It includes trypanothione and trypanothione reductase (TryR) instead of the thioredoxin and glutaredoxin systems of mammalian hosts. Here, we show that the benzisothiazolone compound ebsulfur (EbS), a sulfur analogue of ebselen, is a potent inhibitor of T. brucei growth with a favorable selectivity index over mammalian cells. EbS inhibited the TryR activity and decreased non-protein thiol levels in cultured parasites. The inhibition of TryR by EbS was irreversible and NADPH-dependent. EbS formed a complex with TryR and caused oxidation and inactivation of the enzyme. EbS was more toxic for T. brucei than for Trypanosoma cruzi, probably due to lower levels of TryR and trypanothione in T. brucei. Furthermore, inhibition of TryR produced high intracellular reactive oxygen species. Hydrogen peroxide, known to be constitutively high in T. brucei, enhanced the EbS inhibition of TryR. The elevation of reactive oxygen species production in parasites caused by EbS induced a programmed cell death. Soluble EbS analogues were synthesized and cured T. brucei brucei infection in mice when used together with nifurtimox. Altogether, EbS and EbS analogues disrupt the trypanothione system, hampering the defense against oxidative stress. Thus, EbS is a promising lead for development of drugs against African trypanosomiasis.

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16

Hunter, W. N., M. S. Alphey, C. S. Bond, and A. W. Schüttelkopf. "Targeting metabolic pathways in microbial pathogens: oxidative stress and anti-folate drug resistance in trypanosomatids." Biochemical Society Transactions 31, no. 3 (2003): 607–10. http://dx.doi.org/10.1042/bst0310607.

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The large quantity of genomic, biochemical and metabolic data on microbial pathogens provides information that helps us to select biological problems of interest and to identify targets, metabolic pathways or constituent enzymes, for therapeutic intervention. One area of potential use in developing novel anti-parasitic agents concerns the regulation of oxidative stress, and we have targeted the trypanothione peroxidase pathway in this respect. In order to characterize this pathway, we have determined crystal structures for each of its components, and are now studying enzyme–ligand complexes of the first enzyme, trypanothione reductase. Also with regard to trypanosomatids, a question that arose was: why do anti-folates not provide useful therapies? The enzyme pteridine reductase has been shown to contribute to anti-folate drug resistance, and we have determined the enzyme structure and mechanism to understand this aspect of drug resistance.

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17

Hunter, William N., Keith Smith, Zygmunt Derewenda, et al. "Initiating a crystallographic study of trypanothione reductase." Journal of Molecular Biology 216, no. 2 (1990): 235–37. http://dx.doi.org/10.1016/s0022-2836(05)80314-6.

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18

TAYLOR, M. C., J. M. KELLY, A. H. FAIRLAMB, and M. A. MILES. "The trypanothione reductase gene of Leishmania donovani." Biochemical Society Transactions 18, no. 5 (1990): 869–70. http://dx.doi.org/10.1042/bst0180869.

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19

EL-WAER, ABDUSSALAM F., TIMOTHY BENSON, and KENNETH T. DOUGLAS. "Synthesis of substrate analogues for trypanothione reductase." International Journal of Peptide and Protein Research 41, no. 2 (2009): 141–46. http://dx.doi.org/10.1111/j.1399-3011.1993.tb00124.x.

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20

Aumercier, M., D. Mezianecherif, M. Moutiez, A. Tartar, and C. Sergheraert. "A Microplate Assay for Trypanothione Reductase Inhibitors." Analytical Biochemistry 223, no. 1 (1994): 161–64. http://dx.doi.org/10.1006/abio.1994.1563.

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21

Garrard, Elizabeth A., Emily C. Borman, Brian N. Cook, Emily J. Pike, and David G. Alberg. "Inhibition of Trypanothione Reductase by Substrate Analogues." Organic Letters 2, no. 23 (2000): 3639–42. http://dx.doi.org/10.1021/ol0065423.

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22

Moutiez, M., M. Aumercier, R. Schöneck, et al. "Purification and characterization of a trypanothione-glutathione thioltransferase from Trypanosoma cruzi." Biochemical Journal 310, no. 2 (1995): 433–37. http://dx.doi.org/10.1042/bj3100433.

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Although trypanothione [T(S)2] is the major thiol component in trypanosomatidae, significant amounts of glutathione are present in Trypanosoma cruzi. This could be explained by the existence of enzymes using glutathione or both glutathione and T(S)2 as cofactors. To assess these hypotheses, a cytosolic fraction of T. cruzi epimastigotes was subjected to affinity chromatography columns using as ligands either S-hexylglutathione or a non-reducible analogue of trypanothione disulphide. A similar protein of 52 kDa was eluted in both cases. Its partial amino acid sequence indicated that it was identical with the protein encoded by the TcAc2 cDNA previously described [Schoneck, Plumas-Marty, Taibi et al. (1994) Biol. Cell 80, 1-10]. This protein showed no significant glutathione transferase activity but surprisingly catalysed the thiol-disulphide exchange between dihydrotrypanothione and glutathione disulphide. The kinetic parameters were in the same range as those determined for trypanothione reductase toward its natural substrate. This trypanothione-glutathione thioltransferase provides a new target for a specific chemotherapy against Chagas' disease and may constitute a link between the glutathione-based metabolism of the host and the trypanothione-based metabolism of the parasite.

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23

Ponasik, J. A., C. Strickland, C. Faerman, S. Savvides, P. A. Karplus, and B. Ganem. "Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase." Biochemical Journal 311, no. 2 (1995): 371–75. http://dx.doi.org/10.1042/bj3110371.

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The enzyme trypanothione reductase (TR), together with its substrate, the glutathione-spermidine conjugate trypanothione, plays an essential role in protecting parasitic trypanosomatids against oxidative stress and is a target for drug design. Here we show that a naturally occurring spermine derivative, the antihypertensive agent kukoamine A [N1N12-bis(dihydrocaffeoyl)-spermine] inhibits TR as a mixed inhibitor (Ki = 1.8 microM, Kii = 13 microM). Kukoamine shows no significant inhibition of human glutathione reductase (Ki > 10 mM) and thus provides a novel selective drug lead. The corresponding N1N8-bis(dihydrocaffeoyl)spermidine derivative was synthesized and acted as a purely competitive inhibitor with Ki = 7.5 microM. A series of mono- and di-acylated spermines and spermidines were synthesized to gain an insight into the effect of polyamine chain length, the nature and position of the acyl substituent and the importance of conformational mobility. These compounds inhibited TR with Ki values ranging from 11 to 607 microM.

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24

Lenz, Krauth-Siegel, and Schmidt. "Natural Sesquiterpene Lactones of the 4,15-iso-Atriplicolide Type are Inhibitors of Trypanothione Reductase." Molecules 24, no. 20 (2019): 3737. http://dx.doi.org/10.3390/molecules24203737.

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In the course of our investigations on the antitrypanosomal potential of sesquiterpene lactones (STL), we have recently reported on the exceptionally strong activity of 4,15-iso-Atriplicolide tiglate, which demonstrated an IC50 value of 15 nM against Trypanosoma brucei rhodesiense, the etiologic agent responsible for East African human trypanosomiasis (HAT). Since STLs are known to often interact with their biological targets (e.g., in anti-inflammatory and anti-tumor activity) by means of the covalent modification of biological nucleophiles—most prominently free cysteine thiol groups in proteins—it was a straightforward assumption that such compounds might interfere with the trypanothione-associated detoxification system of trypanosomes. This system heavily relies on thiol groups in the form of the dithiol trypanothione (T(SH)2) and in the active centers of enzymes involved in trypanothione metabolism and homeostasis. Indeed, we found in the present study that 4,15-iso-atriplicolide tiglate, as well as its structural homologues, the corresponding methacrylate and isobutyrate, are inhibitors of trypanothione reductase (TR), the enzyme serving the parasites to keep T(SH)2 in the dithiol state. The TR inhibitory activity was demonstrated to be time-dependent and irreversible. Quite interestingly, of the several further STLs with different core structures that were also tested, none inhibited TR at a significant level. Thus, the TR inhibitory effect by the 4,15-iso-atriplicolide esters appears to be specific for this particular type of furanoheliangolide-type STL. Some structure–activity relationships can already be deduced on the basis of the data reported here, which may serve as the starting point for searching further, possibly more potent, TR inhibitors.

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25

Fournet, Alain, Alba Inchausti, Gloria Yaluff, et al. "Trypanocidal Bisbenzylisoquinoline Alkaloids are Inhibitors of Trypanothione Reductase." Journal of Enzyme Inhibition 13, no. 1 (1998): 1–9. http://dx.doi.org/10.3109/14756369809035823.

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26

Oliveira, Renata B. de, Aline BM Vaz, Rosana O. Alves, et al. "Arylfurans as potential Trypanosoma cruzi trypanothione reductase inhibitors." Memórias do Instituto Oswaldo Cruz 101, no. 2 (2006): 169–73. http://dx.doi.org/10.1590/s0074-02762006000200009.

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27

Dormeyer, Matthias, Nina Reckenfelderbäumer, Heike Lüdemann, and R. Luise Krauth-Siegel. "Trypanothione-dependent Synthesis of Deoxyribonucleotides byTrypanosoma bruceiRibonucleotide Reductase." Journal of Biological Chemistry 276, no. 14 (2001): 10602–6. http://dx.doi.org/10.1074/jbc.m010352200.

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28

Singh, Bishal K., Nandini Sarkar, M. V. Jagannadham, and Vikash K. Dubey. "Modeled structure of trypanothione reductase of Leishmania infantum." BMB Reports 41, no. 6 (2008): 444–47. http://dx.doi.org/10.5483/bmbrep.2008.41.6.444.

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29

CHAN, CECIL, HONG YIN, JACQUI GARFORTH, et al. "Inhibitors of trypanothione reductase as potential antitrypanosomal drugs." Biochemical Society Transactions 23, no. 4 (1995): 511S. http://dx.doi.org/10.1042/bst023511s.

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30

ENTRALA, E., C. MASCARO, and J. BARRETT. "Anti-oxidant enzymes in Cryptosporidium parvum oocysts." Parasitology 114, no. 1 (1997): 13–17. http://dx.doi.org/10.1017/s0031182096008037.

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Oocysts of Cryptosporidium parvum showed relatively low levels of SOD activity. The SOD which had a pI of 4.8 and an approximate molecular weight of 35 kDa appeared to be iron dependent. Catalase, glutathione transferase, glutathione reductase and glutathione peroxidase activity could not be detected, nor could trypanothione reductase. No NADH or NADPH oxidase activity could be detected, nor could peroxidase activity be demonstrated using o-dianisidine, guaiacol, NADPH or NADH as co-substrates. However, an NADPH-dependent H2O2 scavenging system was detected in the insoluble fraction.

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31

Blackie, Margaret A. L., Ahilan Saravanamuthu, Alan H. Fairlamb, and Kelly Chibale. "Inhibition of trypanothione reductase and glutathione reductase by ferrocenic 4-aminoquinoline ureas." Arkivoc 2008, no. 6 (2008): 52–60. http://dx.doi.org/10.3998/ark.5550190.0009.605.

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32

Bradley, Mark, Uwe S. Buecheler, and Christopher T. Walsh. "Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase." Biochemistry 30, no. 25 (1991): 6124–27. http://dx.doi.org/10.1021/bi00239a006.

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33

Iribarne, Federico, Margot Paulino, Sara Aguilera, Miguel Murphy, and Orlando Tapia. "Docking and molecular dynamics studies at trypanothione reductase and glutathione reductase active sites." Journal of Molecular Modeling 8, no. 5 (2002): 173–83. http://dx.doi.org/10.1007/s00894-002-0082-0.

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34

CUNNINGHAM, Mark L., Marketa J. J. M. ZVELEBIL, and Alan H. FAIRLAMB. "Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals." European Journal of Biochemistry 221, no. 1 (1994): 285–95. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18740.x.

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35

Kliukiené, Regina, Audrone Maroziené, Narimantas Cénas, Katja Becker, and John S. Blanchard. "Photoinactivation of Trypanothione Reductase and Glutathione Reductase by A1-Phthalocyanine Tetrasulfonate and Hematoporphyrin." Biochemical and Biophysical Research Communications 218, no. 2 (1996): 629–32. http://dx.doi.org/10.1006/bbrc.1996.0111.

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36

Faerman, Carlos H., Savvas N. Savvides, Corey Strickland, et al. "Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors." Bioorganic & Medicinal Chemistry 4, no. 8 (1996): 1247–53. http://dx.doi.org/10.1016/0968-0896(96)00120-4.

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37

Chitkul, Bordin, and Mark Bradley. "Optimising inhibitors of Trypanothione reductase using solid-phase chemistry." Bioorganic & Medicinal Chemistry Letters 10, no. 20 (2000): 2367–69. http://dx.doi.org/10.1016/s0960-894x(00)00471-6.

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38

Kuriyan, John, Lim Wong, Brian D. Guenther, Nicholas J. Murgolo, Anthony Cerami, and Graeme B. Henderson. "Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata." Journal of Molecular Biology 215, no. 3 (1990): 335–37. http://dx.doi.org/10.1016/s0022-2836(05)80353-5.

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39

Matadamas-Martínez, Félix, Alicia Hernández-Campos, Alfredo Téllez-Valencia, et al. "Leishmania mexicana Trypanothione Reductase Inhibitors: Computational and Biological Studies." Molecules 24, no. 18 (2019): 3216. http://dx.doi.org/10.3390/molecules24183216.

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Leishmanicidal drugs have many side effects, and drug resistance to all of them has been documented. Therefore, the development of new drugs and the identification of novel therapeutic targets are urgently needed. Leishmania mexicana trypanothione reductase (LmTR), a NADPH-dependent flavoprotein oxidoreductase important to thiol metabolism, is essential for parasite viability. Its absence in the mammalian host makes this enzyme an attractive target for the development of new anti-Leishmania drugs. Herein, a tridimensional model of LmTR was constructed and the molecular docking of 20 molecules from a ZINC database was performed. Five compounds (ZINC04684558, ZINC09642432, ZINC12151998, ZINC14970552, and ZINC11841871) were selected (docking scores −10.27 kcal/mol to −5.29 kcal/mol and structurally different) and evaluated against recombinant LmTR (rLmTR) and L. mexicana promastigote. Additionally, molecular dynamics simulation of LmTR-selected compound complexes was achieved. The five selected compounds inhibited rLmTR activity in the range of 32.9% to 40.1%. The binding of selected compounds to LmTR involving different hydrogen bonds with distinct residues of the molecule monomers A and B is described. Compound ZINC12151998 (docking score −10.27 kcal/mol) inhibited 32.9% the enzyme activity (100 µM) and showed the highest leishmanicidal activity (IC50 = 58 µM) of all the selected compounds. It was more active than glucantime, and although its half-maximal cytotoxicity concentration (CC50 = 53 µM) was higher than that of the other four compounds, it was less cytotoxic than amphotericin B. Therefore, compound ZINC12151998 provides a promising starting point for a hit-to-lead process in our search for new anti-Leishmania drugs that are more potent and less cytotoxic.

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Ortalli, Margherita, Andrea Ilari, Gianni Colotti, et al. "Identification of chalcone-based antileishmanial agents targeting trypanothione reductase." European Journal of Medicinal Chemistry 152 (May 2018): 527–41. http://dx.doi.org/10.1016/j.ejmech.2018.04.057.

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41

Fernandez-Gomez, R. "2-Amino diphenylsulfides as new inhibitors of trypanothione reductase." International Journal of Antimicrobial Agents 6, no. 2 (1995): 111–18. http://dx.doi.org/10.1016/0924-8579(95)00029-x.

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Moreno, Silvia N. J., Eva G. S. Carnieri, and Roberto Docampo. "Inhibition of Trypanosoma cruzi trypanothione reductase by crystal violet." Molecular and Biochemical Parasitology 67, no. 2 (1994): 313–20. http://dx.doi.org/10.1016/0166-6851(94)00140-5.

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Krauth-Siegel, R. Luise, and Oliver Inhoff. "Parasite-specific trypanothione reductase as a drug target molecule." Parasitology Research 90 (June 1, 2003): S77—S85. http://dx.doi.org/10.1007/s00436-002-0771-8.

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WILKINSON, Shane R., David J. MEYER, and John M. KELLY. "Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity." Biochemical Journal 352, no. 3 (2000): 755–61. http://dx.doi.org/10.1042/bj3520755.

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Abstract:

In most eukaryotes, glutathione-dependent peroxidases play a key role in the metabolism of peroxides. Numerous studies have reported that trypanosomatids lack this activity. Here we show that this is not the case, at least for the American trypanosome Trypanosoma cruzi. We have isolated a single-copy gene from T. cruzi with the potential to encode an 18kDa enzyme, the sequence of which has highest similarity with glutathione peroxidases from plants. A recombinant form of the protein was purified following expression in Escherichia coli. The enzyme was shown to have peroxidase activity in the presence of glutathione/glutathione reductase but not in the presence of trypanothione/trypanothione reductase. It could metabolize a wide range of hydroperoxides (linoleic acid hydroperoxide and phosphatidylcholine hydroperoxide> cumene hydroperoxide>t-butyl hydroperoxide), but no activity towards hydrogen peroxide was detected. Enzyme activity could be saturated by glutathione when both fatty acid and short-chain organic hydroperoxides were used as substrate. For linoleic acid hydroperoxide, the rate-limiting step of this reaction is the reduction of the peroxidase by glutathione. With lower-affinity substrates such as t-butyl hydroperoxide, the rate-limiting step is the reduction of the oxidant. The data presented here identify a new arm of the T. cruzi oxidative defence system.

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Iribarne, F., M. González, H. Cerecetto, S. Aguilera, O. Tapia, and M. Paulino. "Interaction energies of nitrofurans with trypanothione reductase and glutathione reductase studied by molecular docking." Journal of Molecular Structure: THEOCHEM 818, no. 1-3 (2007): 7–22. http://dx.doi.org/10.1016/j.theochem.2007.04.035.

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da Rocha Pita, Samuel Silva, José Jair Vianna Cirino, Ricardo Bicca de Alencastro, Helena Carla Castro, Carlos Rangel Rodrigues, and Magaly Girão Albuquerque. "Molecular docking of a series of peptidomimetics in the trypanothione binding site of T. cruzi Trypanothione Reductase." Journal of Molecular Graphics and Modelling 28, no. 4 (2009): 330–35. http://dx.doi.org/10.1016/j.jmgm.2009.08.011.

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Chibale, Kelly, and Chitalu Musonda. "The Synthesis of Parasitic Cysteine Protease and Trypanothione Reductase Inhibitors." Current Medicinal Chemistry 10, no. 18 (2003): 1863–89. http://dx.doi.org/10.2174/0929867033456963.

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Kothandan, Ram, Muthusaravanan Sivaramakrishnan, Vivek Jagadeesan Sharavanan, Ramakrishnan Sivasubramanian, and Vinohar Stephen Rapheal. "MOLECULAR DOCKING STUDIES OF PHYTOCHEMICALS AGAINST LEISHMANIA DONOVANI TRYPANOTHIONE REDUCTASE." International Research Journal of Pharmacy 9, no. 1 (2018): 61–65. http://dx.doi.org/10.7897/2230-8407.0919.

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Duyzend, Michael H., Christopher T. Clark, Shayna L. Simmons, et al. "Synthesis and evaluation of substrate analogue inhibitors of trypanothione reductase." Journal of Enzyme Inhibition and Medicinal Chemistry 27, no. 6 (2011): 784–94. http://dx.doi.org/10.3109/14756366.2011.604319.

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Girault, Sophie, Elisabeth Davioud-Charvet, Louis Maes, et al. "Potent and specific inhibitors of trypanothione reductase from Trypanosoma cruzi." Bioorganic & Medicinal Chemistry 9, no. 4 (2001): 837–46. http://dx.doi.org/10.1016/s0968-0896(00)00312-6.

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