ArticleMolecular therapy. Oncology2026
Engineered indoleamine 2,3-dioxygenase variant: Oxidative activation of prodrug indole-3-acetic acid against cancer cells for targeted therapy.
Article in Molecular therapy. Oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme involved in the kynurenine pathway of tryptophan metabolism and has been implicated in immune regulation and tumor immune evasion. Beyond its role in tryptophan metabolism, we found that IDO can catalyze the oxidative activation of indole-3-acetic acid (IAA). This reaction generates reactive oxidative intermediates and triggers potent cytotoxicity in cancer cells. Leveraging human-derived enzymes as "suicide effectors" confers a critical advantage by mitigating the risk of immunogenic rejection. However, the intrinsic kynurenine-pathway activity of wild-type IDO constrains its immediate therapeutic translatability. To surmount this limitation, we further designed and characterized a truncated variant, IDO
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