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Relevant bibliographies by topics / Trypanothion reductase

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Journal articles

Academic literature on the topic 'Trypanothion reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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Journal articles on the topic "Trypanothion reductase"

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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