Pancreatic lipase inhibitory activity of selected pharmaceutical agents
Twenty-five structurally diverse compounds have been tested in vitro for their pancreatic lipase (PL) inhibitory activity. Despite the diversity of tested compounds, the relationship comprising structural attributes of the compounds could be established to correlate with the observed inhibitory acti...
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| Format: | Article |
| Language: | English |
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Sciendo
2019-03-01
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| Series: | Acta Pharmaceutica |
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| Online Access: | https://doi.org/10.2478/acph-2019-0010 |
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| author | Hamdan Imad I. Kasabri Violet N. Al-Hiari Yusuf M. El-Sabawi Dina Zalloum Hiba |
| author_facet | Hamdan Imad I. Kasabri Violet N. Al-Hiari Yusuf M. El-Sabawi Dina Zalloum Hiba |
| author_sort | Hamdan Imad I. |
| collection | DOAJ |
| description | Twenty-five structurally diverse compounds have been tested in vitro for their pancreatic lipase (PL) inhibitory activity. Despite the diversity of tested compounds, the relationship comprising structural attributes of the compounds could be established to correlate with the observed inhibitory activity. Compounds that exerted inhibitory action through surface activity were of different profile from the rest of compounds. When co-incubated with orlistat (OsT), important synergistic effects for some compounds (orphenadrine, gliclazide, cefuroxime and sulfacetamide) were revealed, while antagonistic effects were demonstrated for others (camphor sulfonic acid and dinitro salicylic acid). Docking studies for the most active molecules were performed and molecular interaction forces with the PL active site were identified. The results suggested co-binding of OsT along with the other inhibitor in the binding site in cases of synergistic effect but not in the case of antagonistic effect. These results were additionally supported by affinity capillary electrophoresis. In conclusion, synergistic lipase inhibitory activity between OsT and some other pharmaceutical compounds was demonstrated for the first time, which might help improve the pharmacological effect of OsT. |
| format | Article |
| id | doaj-art-4903d7cc04ae40dfaab61e661f5b2f9b |
| institution | Kabale University |
| issn | 1846-9558 |
| language | English |
| publishDate | 2019-03-01 |
| publisher | Sciendo |
| record_format | Article |
| series | Acta Pharmaceutica |
| spelling | doaj-art-4903d7cc04ae40dfaab61e661f5b2f9b2025-02-02T00:31:54ZengSciendoActa Pharmaceutica1846-95582019-03-0169111610.2478/acph-2019-0010acph-2019-0010Pancreatic lipase inhibitory activity of selected pharmaceutical agentsHamdan Imad I.0Kasabri Violet N.1Al-Hiari Yusuf M.2El-Sabawi Dina3Zalloum Hiba4School of Pharmacy, The University of Jordan, Amman11942, JordanSchool of Pharmacy, The University of Jordan, Amman11942, JordanSchool of Pharmacy, The University of Jordan, Amman11942, JordanSchool of Pharmacy, The University of Jordan, Amman11942, JordanHamdi Mango Centre for Scientific Research, The University of Jordan, Amman11942, JordanTwenty-five structurally diverse compounds have been tested in vitro for their pancreatic lipase (PL) inhibitory activity. Despite the diversity of tested compounds, the relationship comprising structural attributes of the compounds could be established to correlate with the observed inhibitory activity. Compounds that exerted inhibitory action through surface activity were of different profile from the rest of compounds. When co-incubated with orlistat (OsT), important synergistic effects for some compounds (orphenadrine, gliclazide, cefuroxime and sulfacetamide) were revealed, while antagonistic effects were demonstrated for others (camphor sulfonic acid and dinitro salicylic acid). Docking studies for the most active molecules were performed and molecular interaction forces with the PL active site were identified. The results suggested co-binding of OsT along with the other inhibitor in the binding site in cases of synergistic effect but not in the case of antagonistic effect. These results were additionally supported by affinity capillary electrophoresis. In conclusion, synergistic lipase inhibitory activity between OsT and some other pharmaceutical compounds was demonstrated for the first time, which might help improve the pharmacological effect of OsT.https://doi.org/10.2478/acph-2019-0010pancreatic lipasepancreatic lipase inhibitory testpharmaceutical compoundsaffinity capillary electrophoresisdocking studies |
| spellingShingle | Hamdan Imad I. Kasabri Violet N. Al-Hiari Yusuf M. El-Sabawi Dina Zalloum Hiba Pancreatic lipase inhibitory activity of selected pharmaceutical agents Acta Pharmaceutica pancreatic lipase pancreatic lipase inhibitory test pharmaceutical compounds affinity capillary electrophoresis docking studies |
| title | Pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| title_full | Pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| title_fullStr | Pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| title_full_unstemmed | Pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| title_short | Pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| title_sort | pancreatic lipase inhibitory activity of selected pharmaceutical agents |
| topic | pancreatic lipase pancreatic lipase inhibitory test pharmaceutical compounds affinity capillary electrophoresis docking studies |
| url | https://doi.org/10.2478/acph-2019-0010 |
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