Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity
N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural chan...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
de Lucio, Héctor [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles - Jose, Ajay ELSEVIER, 2018, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:244 ; year:2022 ; day:15 ; month:12 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.ejmech.2022.114878 |
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| 245 | 1 | 0 | |a Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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| 520 | |a N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. | ||
| 520 | |a N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. | ||
| 650 | 7 | |a Leishmania infantum |2 Elsevier | |
| 650 | 7 | |a N-alkylation |2 Elsevier | |
| 650 | 7 | |a Dimerization disruptor |2 Elsevier | |
| 650 | 7 | |a Trypanothione disulfide reductase |2 Elsevier | |
| 650 | 7 | |a 1,2,3-Triazolium salts |2 Elsevier | |
| 650 | 7 | |a Competitive inhibitor |2 Elsevier | |
| 700 | 1 | |a Revuelto, Alejandro |4 oth | |
| 700 | 1 | |a Carriles, Alejandra A. |4 oth | |
| 700 | 1 | |a de Castro, Sonia |4 oth | |
| 700 | 1 | |a García-González, Sonia |4 oth | |
| 700 | 1 | |a García-Soriano, Juan Carlos |4 oth | |
| 700 | 1 | |a Alcón-Calderón, Mercedes |4 oth | |
| 700 | 1 | |a Sánchez-Murcia, Pedro A. |4 oth | |
| 700 | 1 | |a Hermoso, Juan A. |4 oth | |
| 700 | 1 | |a Gago, Federico |4 oth | |
| 700 | 1 | |a Camarasa, María-José |4 oth | |
| 700 | 1 | |a Jiménez-Ruiz, Antonio |4 oth | |
| 700 | 1 | |a Velázquez, Sonsoles |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Jose, Ajay ELSEVIER |t Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles |d 2018 |g Amsterdam [u.a.] |w (DE-627)ELV000457477 |
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10.1016/j.ejmech.2022.114878 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001984.pica (DE-627)ELV059488166 (ELSEVIER)S0223-5234(22)00780-2 DE-627 ger DE-627 rakwb eng 570 540 VZ BIODIV DE-30 fid 42.00 bkl de Lucio, Héctor verfasserin aut Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. Leishmania infantum Elsevier N-alkylation Elsevier Dimerization disruptor Elsevier Trypanothione disulfide reductase Elsevier 1,2,3-Triazolium salts Elsevier Competitive inhibitor Elsevier Revuelto, Alejandro oth Carriles, Alejandra A. oth de Castro, Sonia oth García-González, Sonia oth García-Soriano, Juan Carlos oth Alcón-Calderón, Mercedes oth Sánchez-Murcia, Pedro A. oth Hermoso, Juan A. oth Gago, Federico oth Camarasa, María-José oth Jiménez-Ruiz, Antonio oth Velázquez, Sonsoles oth Enthalten in Elsevier Science Jose, Ajay ELSEVIER Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles 2018 Amsterdam [u.a.] (DE-627)ELV000457477 volume:244 year:2022 day:15 month:12 pages:0 https://doi.org/10.1016/j.ejmech.2022.114878 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA 42.00 Biologie: Allgemeines VZ AR 244 2022 15 1215 0 |
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10.1016/j.ejmech.2022.114878 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001984.pica (DE-627)ELV059488166 (ELSEVIER)S0223-5234(22)00780-2 DE-627 ger DE-627 rakwb eng 570 540 VZ BIODIV DE-30 fid 42.00 bkl de Lucio, Héctor verfasserin aut Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. Leishmania infantum Elsevier N-alkylation Elsevier Dimerization disruptor Elsevier Trypanothione disulfide reductase Elsevier 1,2,3-Triazolium salts Elsevier Competitive inhibitor Elsevier Revuelto, Alejandro oth Carriles, Alejandra A. oth de Castro, Sonia oth García-González, Sonia oth García-Soriano, Juan Carlos oth Alcón-Calderón, Mercedes oth Sánchez-Murcia, Pedro A. oth Hermoso, Juan A. oth Gago, Federico oth Camarasa, María-José oth Jiménez-Ruiz, Antonio oth Velázquez, Sonsoles oth Enthalten in Elsevier Science Jose, Ajay ELSEVIER Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles 2018 Amsterdam [u.a.] (DE-627)ELV000457477 volume:244 year:2022 day:15 month:12 pages:0 https://doi.org/10.1016/j.ejmech.2022.114878 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA 42.00 Biologie: Allgemeines VZ AR 244 2022 15 1215 0 |
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10.1016/j.ejmech.2022.114878 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001984.pica (DE-627)ELV059488166 (ELSEVIER)S0223-5234(22)00780-2 DE-627 ger DE-627 rakwb eng 570 540 VZ BIODIV DE-30 fid 42.00 bkl de Lucio, Héctor verfasserin aut Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. Leishmania infantum Elsevier N-alkylation Elsevier Dimerization disruptor Elsevier Trypanothione disulfide reductase Elsevier 1,2,3-Triazolium salts Elsevier Competitive inhibitor Elsevier Revuelto, Alejandro oth Carriles, Alejandra A. oth de Castro, Sonia oth García-González, Sonia oth García-Soriano, Juan Carlos oth Alcón-Calderón, Mercedes oth Sánchez-Murcia, Pedro A. oth Hermoso, Juan A. oth Gago, Federico oth Camarasa, María-José oth Jiménez-Ruiz, Antonio oth Velázquez, Sonsoles oth Enthalten in Elsevier Science Jose, Ajay ELSEVIER Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles 2018 Amsterdam [u.a.] (DE-627)ELV000457477 volume:244 year:2022 day:15 month:12 pages:0 https://doi.org/10.1016/j.ejmech.2022.114878 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA 42.00 Biologie: Allgemeines VZ AR 244 2022 15 1215 0 |
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10.1016/j.ejmech.2022.114878 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001984.pica (DE-627)ELV059488166 (ELSEVIER)S0223-5234(22)00780-2 DE-627 ger DE-627 rakwb eng 570 540 VZ BIODIV DE-30 fid 42.00 bkl de Lucio, Héctor verfasserin aut Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. Leishmania infantum Elsevier N-alkylation Elsevier Dimerization disruptor Elsevier Trypanothione disulfide reductase Elsevier 1,2,3-Triazolium salts Elsevier Competitive inhibitor Elsevier Revuelto, Alejandro oth Carriles, Alejandra A. oth de Castro, Sonia oth García-González, Sonia oth García-Soriano, Juan Carlos oth Alcón-Calderón, Mercedes oth Sánchez-Murcia, Pedro A. oth Hermoso, Juan A. oth Gago, Federico oth Camarasa, María-José oth Jiménez-Ruiz, Antonio oth Velázquez, Sonsoles oth Enthalten in Elsevier Science Jose, Ajay ELSEVIER Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles 2018 Amsterdam [u.a.] (DE-627)ELV000457477 volume:244 year:2022 day:15 month:12 pages:0 https://doi.org/10.1016/j.ejmech.2022.114878 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA 42.00 Biologie: Allgemeines VZ AR 244 2022 15 1215 0 |
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10.1016/j.ejmech.2022.114878 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001984.pica (DE-627)ELV059488166 (ELSEVIER)S0223-5234(22)00780-2 DE-627 ger DE-627 rakwb eng 570 540 VZ BIODIV DE-30 fid 42.00 bkl de Lucio, Héctor verfasserin aut Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. Leishmania infantum Elsevier N-alkylation Elsevier Dimerization disruptor Elsevier Trypanothione disulfide reductase Elsevier 1,2,3-Triazolium salts Elsevier Competitive inhibitor Elsevier Revuelto, Alejandro oth Carriles, Alejandra A. oth de Castro, Sonia oth García-González, Sonia oth García-Soriano, Juan Carlos oth Alcón-Calderón, Mercedes oth Sánchez-Murcia, Pedro A. oth Hermoso, Juan A. oth Gago, Federico oth Camarasa, María-José oth Jiménez-Ruiz, Antonio oth Velázquez, Sonsoles oth Enthalten in Elsevier Science Jose, Ajay ELSEVIER Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles 2018 Amsterdam [u.a.] (DE-627)ELV000457477 volume:244 year:2022 day:15 month:12 pages:0 https://doi.org/10.1016/j.ejmech.2022.114878 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA 42.00 Biologie: Allgemeines VZ AR 244 2022 15 1215 0 |
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Enthalten in Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles Amsterdam [u.a.] volume:244 year:2022 day:15 month:12 pages:0 |
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Enthalten in Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles Amsterdam [u.a.] volume:244 year:2022 day:15 month:12 pages:0 |
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Leishmania infantum N-alkylation Dimerization disruptor Trypanothione disulfide reductase 1,2,3-Triazolium salts Competitive inhibitor |
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Electrochemical synthesis, photodegradation and antibacterial properties of PEG capped zinc oxide nanoparticles |
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de Lucio, Héctor @@aut@@ Revuelto, Alejandro @@oth@@ Carriles, Alejandra A. @@oth@@ de Castro, Sonia @@oth@@ García-González, Sonia @@oth@@ García-Soriano, Juan Carlos @@oth@@ Alcón-Calderón, Mercedes @@oth@@ Sánchez-Murcia, Pedro A. @@oth@@ Hermoso, Juan A. @@oth@@ Gago, Federico @@oth@@ Camarasa, María-José @@oth@@ Jiménez-Ruiz, Antonio @@oth@@ Velázquez, Sonsoles @@oth@@ |
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Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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identification of 1,2,3-triazolium salt-based inhibitors of leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. |
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N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. |
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N-methylation of the triazole moiety present in our recently described triazole-phenyl-thiazole dimerization disruptors of Leishmania infantum trypanothione disulfide reductase (LiTryR) led to a new class of potent inhibitors that target different binding sites on this enzyme. Subtle structural changes among representative library members modified their mechanism of action, switching from models of classical competitive inhibition to time-dependent mixed noncompetitive inhibition. X-ray crystallography and molecular modeling results provided a rationale for this distinct behavior. The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. Of note, L. infantum promastigotes treated with 4c significantly reduced their low-molecular-weight thiol content, thus providing additional evidence that LiTryR is the main target of this novel compound. |
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Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity |
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The remarkable potency and selectivity improvements, particularly against intracellular amastigotes, of the LiTryR dimerization disruptors 4c and 4d reveal that they could be exploited as leishmanicidal agents. 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