<abstract xmlns="http://www.w3.org/1999/xhtml"><p>Twenty-five structurally diverse compounds have been tested <italic>in vitro</italic> 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.</p></abstract>

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.

Pancreatic lipase inhibitory activity of selected pharmaceutical agents

Hamdi Mango Centre for Scientific Research

Acta Pharmaceutica

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

{"article-title":"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...

Pancreatic lipase inhibitory activity of selected pharmaceutical agents

Pubblicato online: 07 dic 2018

Pagine: 1 - 16

Accettato: 24 set 2018

DOI: https://doi.org/10.2478/acph-2019-0010

Parole chiave
pancreatic lipase, pancreatic lipase inhibitory test, pharmaceutical compounds, affinity capillary electrophoresis, docking studies

© 2019 Imad I. Hamdan et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Pancreatic lipase inhibitory activity of selected pharmaceutical agents

Pubblicato online: 07 dic 2018

Pagine: 1 - 16

Accettato: 24 set 2018

DOI: https://doi.org/10.2478/acph-2019-0010

Parole chiavepancreatic lipase, pancreatic lipase inhibitory test, pharmaceutical compounds, affinity capillary electrophoresis, docking studies

© 2019 Imad I. Hamdan et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Parole chiave
pancreatic lipase, pancreatic lipase inhibitory test, pharmaceutical compounds, affinity capillary electrophoresis, docking studies