Literature DB >> 10821719

Structure-activity study on the in vitro antiprotozoal activity of glutathione derivatives.

C D'Silva1, S Daunes.   

Abstract

A series of N-, S-, and COOH-blocked glutathione derivatives were evaluated against the pathogenic parasites Trypanosoma brucei, Trypanosoma cruzi, and Leishmania donovani in vitro, to identify the determinants necessary for activity and for further development into an active lead structure. The results show that N,S-blocked glutathione diesters are the most effective inhibitors of T. brucei with structures 14-16 being the most active, 14 having an IC(50) approximately 1.9 microM. The toxicity effects observed for glutathione derivatives 12, 14, and 16 have been correlated to the K562 antileukemic activity of these compounds and their inhibitory effects on the glyoxalase system of the host. Diester compounds based on S-2,4-dinitrophenylglutathione (17-22) were found to be significantly better inhibitors of T. brucei with ED(50)'s in the range 16-0.19 microM. Compounds 19 and 20 were the two best inhibitors, with an ED(50) of approximately 1.07 and 0.19 microM, respectively; however 20 displayed toxicity in parasitic assays. Monoesters, monoamides, and diamides tested generally exhibited low in vitro activity. The compounds did not inhibit glutathionylspermidine synthetase and trypanothione reductase enzyme targets in the unique trypanothione pathway of these parasites. Diester compounds per se were considered to be ineffective inhibitors of trypanothione metabolism suggesting that these compounds might act as prodrugs, being hydrolyzed in situ into a variety of glutathione derivatives which include combinations of monoesters, free acids, and amines, some of which are inhibitors of trypanothione metabolism.

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Year:  2000        PMID: 10821719     DOI: 10.1021/jm990259w

Source DB:  PubMed          Journal:  J Med Chem        ISSN: 0022-2623            Impact factor:   7.446


  13 in total

1.  Structure-property correlation and estimation of the antiparasitic activity of glutathione derivatives.

Authors:  I B Golovanov; S M Zhenodarova; G R Ivanitskii; M I Khabarova
Journal:  Dokl Biochem Biophys       Date:  2002 Nov-Dec       Impact factor: 0.788

2.  Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs.

Authors:  Prasad K Padmanabhan; Angana Mukherjee; Rentala Madhubala
Journal:  Biochem J       Date:  2006-01-01       Impact factor: 3.857

3.  Glutathione derivatives active against Trypanosoma brucei rhodesiense and T. brucei brucei in vitro.

Authors:  Sylvie Daunes; Claudius D'Silva
Journal:  Antimicrob Agents Chemother       Date:  2002-02       Impact factor: 5.191

4.  A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus.

Authors:  A Sommer; P Fischer; K Krause; K Boettcher; P M Brophy; R D Walter; E Liebau
Journal:  Biochem J       Date:  2001-02-01       Impact factor: 3.857

5.  A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major.

Authors:  Tim J Vickers; Neil Greig; Alan H Fairlamb
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-25       Impact factor: 11.205

6.  Ensemble learning application to discover new trypanothione synthetase inhibitors.

Authors:  Juan I Alice; Carolina L Bellera; Diego Benítez; Marcelo A Comini; Pablo R Duchowicz; Alan Talevi
Journal:  Mol Divers       Date:  2021-07-15       Impact factor: 2.943

Review 7.  Methylglyoxal metabolism in trypanosomes and leishmania.

Authors:  Susan Wyllie; Alan H Fairlamb
Journal:  Semin Cell Dev Biol       Date:  2011-02-15       Impact factor: 7.727

8.  Neglected disease - african sleeping sickness: recent synthetic and modeling advances.

Authors:  Sarvesh K Paliwal; Ankita Narayan Verma; Shailendra Paliwal
Journal:  Sci Pharm       Date:  2011-05-10

9.  Glyoxalase I gene deletion mutants of Leishmania donovani exhibit reduced methylglyoxal detoxification.

Authors:  Swati C Chauhan; Rentala Madhubala
Journal:  PLoS One       Date:  2009-08-27       Impact factor: 3.240

10.  Identification of Novel Chemical Scaffolds Inhibiting Trypanothione Synthetase from Pathogenic Trypanosomatids.

Authors:  Diego Benítez; Andrea Medeiros; Lucía Fiestas; Esteban A Panozzo-Zenere; Franziska Maiwald; Kyriakos C Prousis; Marina Roussaki; Theodora Calogeropoulou; Anastasia Detsi; Timo Jaeger; Jonas Šarlauskas; Lucíja Peterlin Mašič; Conrad Kunick; Guillermo R Labadie; Leopold Flohé; Marcelo A Comini
Journal:  PLoS Negl Trop Dis       Date:  2016-04-12
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