Tag Archives: pancreatic lipase
Inhibition of human pancreatic lipase by aspirin: experimental and in silico study
R. T. Altaee, M. G. Aldabbagh, O. Y. Al-Abbasy
Department of Chemistry, College of Education for Pure Sciences, University of Mosul, Iraq;
*e-mail: chem.omar1978@uomosul.edu.iq
Received: 09 January 2026; Revised: 29 January 2026;
Accepted: 03 April 2026; Available on-line: 21 April 2026
Excessive accumulation of adipose tissue is a hallmark of obesity as a critical factor in the development of numerous chronic medical problems. Pancreatic lipase (PLase), which controls the absorption of fats in the intestine, has gained significance as a target in anti-obesity therapy. This study aimed to evaluate the potential effects of Aspirin as a PLase inhibitor and a weight-loss agent compared to the commonly used anti-obesity drug Xenical. Pancreatic lipase was purified 28.5-fold from the plasma of obese male volunteers using ion-exchange chromatography. Enzyme activity was evaluated using p-nitrophenyl butyrate as a substrate. The kinetic analysis of Aspirin effect on purified enzyme activity revealed a competitive inhibition mechanism with Ki of 24.3 mM. In vivo studies were performed using 20 male Wistar rats randomly divided into four equal groups provided with: 1 – control conditions; 2 – high-fat diet (HFD) for 12 weeks; 3 – HFD and Xenical orally (10 mg/kg BW daily); 4 – HFD and Aspirin orally (14.4 mg/kg BW daily). In an HFD group, increased animals body weight and elevated PLase activity in plasma compared to the control were demonstrated. Treatment with both Aspirin and Xenical resulted in a significant decrease in body weight and PLase activity compared with untreated HFD rats. Molecular docking of Human Pancreatic lipase-related protein 1 (PDB ID: 2PPL) binding with Aspirin and Xenical showed the values of binding energy (ΔG) 5.4 and -4.4 kcal/mol, respectively, indicating a stronger protein interaction with Aspirin compared to Xenical. This combined study reinforces the conclusion that Aspirin has the potential to be a novel anti-obesity agent.
In vivo, in vitro, and molecular docking study of rat pancreatic lipase inhibition using isopropyl salicylate
Noor M. Mahdi1, Sarah A. Younus2,
Abdallah F. Al-Burgus1, Omar Y. Al-Abbasy3*
1General Directorate of Education in Nineveh, Mosul, Iraq;
2Department of Chemistry and Biochemistry, College of Medicine,
University of Nineveh, Mosul, Iraq;
3Department of Chemistry, College of Education for Pure Science,
University of Mosul, Mosul, Iraq;
*e-mail: chem.omar1978@uomosul.edu.iq
Received: 30 April 2025; Revised: 11 July 2025;
Accepted: 12 September 2025; Available on-line: 17 September 2025
Pancreatic lipase (PL) represents a significant treatment target that has been the focus of research on anti-obesity medications. Orlistat is the only regularly used prescription that has been approved for long-term use. The discovery of new compounds for anti-obesity treatment based on PL inhibition can be achieved, in particular, by structure-based virtual screening with docking software. The aim of this research was to study isopropyl salicylate (IPS) anti-hyperlipidemic activity and inhibitory effect on rat pancreatic PL in comparison with orlistat. Wistar rats were divided into four groups of 8 animals each: control; fed with a high-fat diet (HFD) for 12 weeks to produce hyperlipidemia; fed with HFD and Orlistat (10 mg/kg BW daily); fed with HFD and IPS (10.81 mg/kg BW daily). It was shown that BW gain and lipase activity in the plasma of the high-fat diet rats treated with either orlistat or isopropyl salicylate were reduced considerably compared with untreated rats. The pancreatic lipase was partially purified from the plasma of obese rats, and a kinetic study of the IPS effect identified a competitive inhibition mode with an assessed Ki of 30.53 mM. An in silico study of the interaction between IPS and rat pancreatic lipase-related protein 2 (PDB ID: 1BU8) was conducted. The binding energy value ΔG for the IPS-protein complex at the enzyme’s active site was found to be -5.4 kcal/mol, while that for the orlistat-protein complex was -4.4 kcal/mol, indicating the stronger interaction of the enzyme with isopropyl salicylate than with orlistat.