Mapping Methodological Heterogeneity in Biochemical Assays of Non-Covalent DprE1 Inhibitors: A Systematic Review
Le résumé fourni par la source
Decaprenylphosphoryl-β-D-ribose 2′-epimerase (DprE1) is an essential enzyme involved in mycobacterial cell-wall biosynthesis and a validated target for antituberculosis drug discovery. However, substantial variation in biochemical assay conditions may limit the comparability and interpretation of reported inhibitory activities. This systematic review aims to identify and map the methodological heterogeneity of in vitro biochemical assays used to evaluate non-covalent DprE1 inhibitors. Searches were conducted in PubMed, Scopus, and Web of Science for original research articles published between January 1, 2008, and July 15, 2026. Eligible studies must report quantitative biochemical IC50 values for non-covalent DprE1 inhibitors and provide sufficient information about the experimental protocol. Methodological variables, including enzyme species, protein form, expression system, substrate and cofactor concentrations, buffer composition, pH, detergent, incubation conditions, assay format, and detection method, are being extracted and standardized. The expected outcomes are a systematic characterization of assay heterogeneity, a taxonomy of experimental protocols, and a curated dataset supporting the comparison and interpretation of DprE1 inhibitory activity.
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