ArticlePharmaceutical research2026
Utility of Relative Activity Factors to Determine Fraction Glucuronidation and Clearance of Icenticaftor in Humans.
Article in Pharmaceutical research, 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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4 authors.
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Abstract
purposeThe purpose of this study is to quantify the contribution of individual UDP-glucuronosyl transferase (UGT) enzymes involved in the glucuronidation of icenticaftor, which is primarily glucuronidated in the human liver to two distinct glucuronide metabolites that are ultimately excreted in the urine.
methodsThe formation of icenticaftor-glucuronide in recombinant UGT systems was scaled with relative activity factor (RAF) of involved UGT enzymes to determine the fraction glucuronidation in human liver.
resultsScaling of the glucuronidation activity of UGT enzymes in recombinant UGT systems demonstrated that hepatic UGT1A9 contributed to about two-third of the overall icenticaftor glucuronidation while the remaining was accounted by UGT2B7. Moreover, the predicted UGT-mediated clearance of icenticaftor, upon scaling the intrinsic clearance (CL
conclusionCollectively, current data are indicative of the utility of activity-based scalars to predict fraction glucuronidation and clearance of icenticaftor in the clinic. UGT1A9 is identified as the major UGT enzyme in the glucuronidation of icenticaftor in human liver.
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