Exploring phytochemicals and antidiabetic property of the hexane extract from Abutilon indicum (L.) Sweet roots

The roots of Abutilon indicum (L.) Sweet were extracted with hexane and subjected to bioassay-guided fractionation to evaluate α-glucosidase inhibitory activity. The hexane extract (RAIH, 0.80% w w-1) showed potent inhibition (88.06%) at 500 mg mL-1. Silica gel chromatography localized the activity to fractions RAIH2–RAIH4 (93.55–95.19% inhibition). Chromatographic separation of the bioactive fractions afforded four known sterol-type constituents, identified by IR, 1H NMR, and 13C NMR, and compared with previously reported data as β-sitosterol (1), stigmasterol (2), daucosterol (3), and stigmasterol-3-O-β-D-glucoside (4). Compounds 3 and 4 were isolated from A. indicum for the first time. Although compounds 1–4 were not assayed for α-glucosidase inhibitory activity in this study, literature data indicate that sterol glycosides are more potent than free sterols. Molecular docking was performed, exhibiting stronger binding for 3 and 4 than for 1 and 2, consistent with a contributory role of sugar moieties. These findings support further compound-level validation. Therefore, investigating this plant and its chemical constituents may enhance the discovery of antidiabetic agents and related therapeutic leads. Collectively, these findings challenge the prevailing focus on polar phenolics as primary α-glucosidase inhibitors and highlight sterol-rich, non-polar fractions as an underexplored yet promising source of antidiabetic leads. This study provides a conceptual framework for expanding enzyme-based antidiabetic screening toward lipophilic phytochemical classes and supports further compound-level validation. GRAPHICAL ABSTRACT HIGHLIGHTS Bioassay-guided silica gel fractionation localized activity to fractions RAIH2–RAIH4 of 93.55–95.19% inhibition at 500 mg/mL. Daucosterol and stigmasterol-3-O-β-D-glucoside were isolated for the first time from Abutilon indicum (L.) Molecular docking with yeast α-glucosidase predicted stronger binding for sterol glycosides relative to sterols, supporting the potential role of sugar moieties in enzyme engagement.