ArticleTranslational cancer research2022
Expression, purification, and kinetic characterization of the human strep-IDO1.
Article in Translational cancer research, 2022. 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
Background: Tryptophan catabolism leading to T cell suppression mediated by indoleamine 2,3-dioxygenase (IDO1) is an important mechanism of tumor immune escape, and IDO1 inhibitors have attracted increasing attention as anticancer therapeutics. However, the phase III clinical trial (ECHO-301/KEYNOTE-252) of epacadostat (INCB024360) had disappointing outcomes. This revealed that purification of IDO1 with high purity is one of the major constraints that limit the development of its inhibitors. Methods: Pan-cancer analysis was used to elucidate the relationship between IDO1 function in tumor immunology. The recombinant pET28a-IDO1-strep plasmid and Results: We described an improved method for the purification of recombinant IDO1 protein based on the strep-tag using an Conclusions: Purified human strep-IDO1 using the protocol described in our study could be used for further biochemical and structural analyses, which may facilitate functional research and further drug screening study on IDO1.
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