Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: Substitution of the glycine part

Katie Amssoms, Sandra L. Oza, Koen Augustyns, Abdellah Yamani, Anne-Marie Lambeir, Gunther Bal, Pieter Van der Veken, Alan H. Fairlamb, Achiel Haemers (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    20 Citations (Scopus)

    Abstract

    Glutathionylspermidine synthetase (GspS) is an essential enzyme in the biosynthesis of trypanothione and is an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-X) where the glycine moiety has been substituted for other amino acids. These peptides were evaluated as substrates and inhibitors of GspS. Compounds with basic side chains such as diaminopropionic acid were found to be good inhibitors (Ki: 7.2 μM). Substitution of the glycine part abolished the GspS substrate properties of the tripeptide.

    Original languageEnglish
    Pages (from-to)2703-2705
    Number of pages3
    JournalBioorganic and Medicinal Chemistry Letters
    Volume12
    Issue number19
    DOIs
    Publication statusPublished - 7 Oct 2002

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