JPC-JOURNAL OF PLANAR CHROMATOGRAPHY-MODERN TLC, 2025 (SCI-Expanded)
This study investigates the pancreatic lipase inhibitory activity of oleogum resins from various Boswellia species, integrating high-performance thin-layer chromatography (HPTLC)-effect-directed analysis (EDA) with molecular docking to evaluate bioactive compounds. Pancreatic lipase, a key enzyme in dietary fat digestion, is a crucial target in anti-obesity therapies. HPTLC-EDA revealed that 3-acetyl-11-keto-beta-boswellic acid (AKBA), beta-boswellic acid (BA), and 3-acetyl-beta-boswellic acid (ABA) exhibited notable inhibitory activities, indicated by distinct inhibition zones on HPTLC bioautograms. Among the species tested, Boswellia serrata demonstrated the strongest inhibitory potential, while Boswellia frereana and Boswellia neglecta showed limited activity. Molecular docking studies supported these findings by elucidating the binding interactions of AKBA, BA, and ABA with the pancreatic lipase (PDB ID: 1ETH). The hydrogen bond(s) with Lys81 and/or Arg112 were found to be responsible for the inhibitory effects of AKBA, BA, and ABA on the pancreatic lipase. Unlike orlistat, AKBA, BA, and ABA could not establish hydrogen bonds with three pivotal residues (Ser153, Gly77, and His152), and therefore their lower inhibitory effects may be related to the lack of these binding interactions. These findings suggest that, while Boswellia-derived compounds show promise as natural lipase inhibitors, structural optimization may be required to enhance their potency.