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Model Studies on Peroxidic Glutathione Transferase (GST) Inhibitors: C5‐Methylated 1,2,4‐Trioxanes with C6‐Acrylate Side Chains (Eur. J. Org. Chem. 20/2015)
Author(s) -
Griesbeck Axel G.,
Maaßen Andreas,
Bräutigam Maria,
Pietsch Markus
Publication year - 2015
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201590054
Subject(s) - chemistry , glutathione , stereochemistry , enzyme , moiety , transferase , combinatorial chemistry , biochemistry
The cover picture shows the experimental setup of the key step in the preparation of new peroxidic glutathione transferase (GST) inhibitors, i.e. the regioselective photooxygenation of an allylic alcohol to the respective hydroperoxide. The 1,2,4‐trioxane moiety is then formed by peroxyacetalization with aldehydes, orthoesters, or acetals under boron, indium, and PPTS catalysis, respectively. Inhibition of human GSTP1 (a phase II metabolizing enzyme detoxifying xenobiotics and endogenous compounds, PDB: 5GSS), as found for the new peroxides, is crucial to overcome the drug resistance and antiapoptotic effects mediated by this enzyme in cancer cells (DNA double helix, PDB: 4HLI). Details are discussed in the article by A. G. Griesbeck et al. on 4349 ff . A. G. G., M. B. and M. P. thank the Graduate Program in Pharmacology and Experimental Therapeutics at the University of Cologne and Bayer Healthcare for financial support.