Synthesis and activity of the glutathione analogue gamma-(L-gamma-oxaglutamyl)-L-cysteinyl-glycine.

Paper

Synthesis and activity of the glutathione analogue gamma-(L-gamma-oxaglutamyl)-L-cysteinyl-glycine.

Published 1996 · A. Calcagni, S. Dupré, G. Lucente

Archiv der Pharmazie

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2

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0

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Abstract

An efficient synthesis of the backbone modified glutathione analogue gamma-(L-gamma-oxaglutamyl)-L-cysteinyl-glycine (7), characterized by the presence of an urethane O-CO-NH linkage replacing the gamma-glutamylic CH2CO-NH fragment is described. The new analogue has been fully characterized by 1H- and 13C-NMR, and FAB-MS. Compound 7 was tested for inhibition of gamma-glutamyl-transferase activity and was found to be a non-competitive inhibitor of hog kidney gamma-glutamyltransferase (EC 2.3.2.2).

In Vitro Study

Study Snapshot

The modified glutathione analogue gamma-(L-gamma-oxaglutamyl)-L-cysteinyl-glycine (7) is a non-competitive inhibitor of hog kidney gamma-glutamyltransferase

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Synthesis and activity of the glutathione analogue gamma-(L-gamma-oxaglutamyl)-L-cysteinyl-glycine.

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References

Citations

Coumarin-Based Dual Inhibitors of Human Carbonic Anhydrases and Monoamine Oxidases Featuring Amino Acyl and (Pseudo)-Dipeptidyl Appendages: In Vitro and Computational Studies

Coumarin-based compounds show potential as anticancer agents by selectively inhibiting membrane-anchored human carbonic anhydrases and human monoamine oxidases, with compound 6 showing potential as a lead compound.

GLUTATHIONE CONJUGATES AND THEIR SYNTHETIC DERIVATIVES AS INHIBITORS OF GLUTATHIONE-DEPENDENT ENZYMES INVOLVED IN CANCER AND DRUG RESISTANCE

GSH-conjugates and synthetic analogs can inhibit glutathione-dependent enzymes involved in cancer and drug resistance, potentially offering a new treatment strategy.