Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group
Glutathionylspermidine synthetase/amidase (GspS) is an essential enzyme in the biosynthesis and turnover of trypanothione and represents an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-Gly-X) where the glycine...
Guardado en:
| Autores principales: | , , , , , , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0960894X_v12_n18_p2553_Amssoms |
| Aporte de: |
| id |
todo:paper_0960894X_v12_n18_p2553_Amssoms |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_0960894X_v12_n18_p2553_Amssoms2023-10-03T15:53:58Z Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group Amssoms, K. Oza, S.L. Ravaschino, E. Yamani, A. Lambeir, A.-M. Rajan, P. Bal, G. Rodriguez, J.B. Fairlamb, A.H. Augustyns, K. Haemers, A. acylsulfonamide amide boronic acid derivative carboxylic acid enzyme inhibitor glutathione glutathione derivative glutathionylspermidine synthethase glycine hydroxamic acid synthetase tetrazole derivative tripeptide unclassified drug acidity amino acid substitution amino acid synthesis article IC 50 protein analysis Amide Synthases Carboxylic Acids Enzyme Inhibitors Glutathione Glycine Oligopeptides Glutathionylspermidine synthetase/amidase (GspS) is an essential enzyme in the biosynthesis and turnover of trypanothione and represents an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-Gly-X) where the glycine carboxylic acid group (X) has been substituted for other acidic groups such as tetrazole, hydroxamic acid, acylsulphonamide and boronic acid. The boronic acid appears the most promising lead compound (IC50 of 17.2 μM). © 2002 Elsevier Science Ltd. All rights reserved. Fil:Ravaschino, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Rodriguez, J.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0960894X_v12_n18_p2553_Amssoms |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
acylsulfonamide amide boronic acid derivative carboxylic acid enzyme inhibitor glutathione glutathione derivative glutathionylspermidine synthethase glycine hydroxamic acid synthetase tetrazole derivative tripeptide unclassified drug acidity amino acid substitution amino acid synthesis article IC 50 protein analysis Amide Synthases Carboxylic Acids Enzyme Inhibitors Glutathione Glycine Oligopeptides |
| spellingShingle |
acylsulfonamide amide boronic acid derivative carboxylic acid enzyme inhibitor glutathione glutathione derivative glutathionylspermidine synthethase glycine hydroxamic acid synthetase tetrazole derivative tripeptide unclassified drug acidity amino acid substitution amino acid synthesis article IC 50 protein analysis Amide Synthases Carboxylic Acids Enzyme Inhibitors Glutathione Glycine Oligopeptides Amssoms, K. Oza, S.L. Ravaschino, E. Yamani, A. Lambeir, A.-M. Rajan, P. Bal, G. Rodriguez, J.B. Fairlamb, A.H. Augustyns, K. Haemers, A. Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| topic_facet |
acylsulfonamide amide boronic acid derivative carboxylic acid enzyme inhibitor glutathione glutathione derivative glutathionylspermidine synthethase glycine hydroxamic acid synthetase tetrazole derivative tripeptide unclassified drug acidity amino acid substitution amino acid synthesis article IC 50 protein analysis Amide Synthases Carboxylic Acids Enzyme Inhibitors Glutathione Glycine Oligopeptides |
| description |
Glutathionylspermidine synthetase/amidase (GspS) is an essential enzyme in the biosynthesis and turnover of trypanothione and represents an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-Gly-X) where the glycine carboxylic acid group (X) has been substituted for other acidic groups such as tetrazole, hydroxamic acid, acylsulphonamide and boronic acid. The boronic acid appears the most promising lead compound (IC50 of 17.2 μM). © 2002 Elsevier Science Ltd. All rights reserved. |
| format |
JOUR |
| author |
Amssoms, K. Oza, S.L. Ravaschino, E. Yamani, A. Lambeir, A.-M. Rajan, P. Bal, G. Rodriguez, J.B. Fairlamb, A.H. Augustyns, K. Haemers, A. |
| author_facet |
Amssoms, K. Oza, S.L. Ravaschino, E. Yamani, A. Lambeir, A.-M. Rajan, P. Bal, G. Rodriguez, J.B. Fairlamb, A.H. Augustyns, K. Haemers, A. |
| author_sort |
Amssoms, K. |
| title |
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| title_short |
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| title_full |
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| title_fullStr |
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| title_full_unstemmed |
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group |
| title_sort |
glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. part 1: substitution of the glycine carboxylic acid group |
| url |
http://hdl.handle.net/20.500.12110/paper_0960894X_v12_n18_p2553_Amssoms |
| work_keys_str_mv |
AT amssomsk glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT ozasl glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT ravaschinoe glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT yamania glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT lambeiram glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT rajanp glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT balg glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT rodriguezjb glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT fairlambah glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT augustynsk glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup AT haemersa glutathioneliketripeptidesasinhibitorsofglutathionylspermidinesynthetasepart1substitutionoftheglycinecarboxylicacidgroup |
| _version_ |
1782026123506352128 |