The aim is to explore the directed C–H activation of 13α-estrone to develop potential inhibitors for AKR1C isoenzymes.
Conducted molecular docking studies to identify binding affinities of compounds.
Performed biological assays to test the efficacy of AKR1C inhibitors.
Analyzed the modulation of steroid hormone availability.
Identified novel compounds with significant inhibitory activity against AKR1C isoenzymes.
Demonstrated effective modulation of steroid hormone signaling pathways.
Abstract
The aldo-keto reductase isoenzymes AKR1C1–3 regulate local steroid hormone availability through the interconversion of active and inactive ligands, thereby modulating prereceptor signaling.