Sihem Snini
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Sihem Snini has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
- Abdelkarim Abousalham
Université Lyon 1, CNRS, ICBMS, UMR 5246, Villeurbanne, France
2 shared publications - Ahmed Aloulou
Laboratory of Biochemistry and Enzymatic Engineering of Lipases, National Engineering School of Sfax, University of Sfax, Sfax 3038, Tunisia
2 shared publications - Alexandre Noiriel
Université Lyon 1, CNRS, ICBMS, UMR 5246, Villeurbanne, France
2 shared publications - Jannet Kamoun
Laboratory of Biochemistry and Enzymatic Engineering of Lipases, National Engineering School of Sfax, University of Sfax, Sfax 3038, Tunisia
2 shared publications - Michele Fiore
Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, UMR5246, CNRS, Université Claude Bernard Lyon 1, Villeurbanne, France
2 shared publications - Mohamed Sellami
Laboratory of Biochemistry and Enzymatic Engineering of Lipases, National Engineering School of Sfax, University of Sfax, Sfax 3038, Tunisia
2 shared publications
Latest Publications
- Open Access
Identification of an Inhibitory Fraction from Cinnamomum cassia Against Digestive Lipases
Natural inhibitors of digestive lipases offer promising alternatives to conventional obesity medications. This study screened nine medicinal plant extracts, identifying the ethanolic bark extract of Cinnamomum cassia as the most potent inhibitor for gastric and pancreatic lipases. Using an integrated approach combining bioactivity-guided fractionation and mass spectrometry, we isolated the highly active fraction, F3-1-1, which exhibited dose- and time-dependent inhibitory effects against human and porcine pancreatic lipases, as well as dog gastric lipase (DGL). Further mass spectrometry and peptide mass fingerprint analysis putatively annotated cinncassiol A-19 glucoside as a bioactive constituent. Notably, this compound was likely bound covalently to the catalytic peptide containing the Ser153 residue in DGL, characterized by a mass shift of +553.10 Da. Molecular docking simulations supported these suggestions, demonstrating stable interactions within the catalytic pocket of DGL through hydrogen and hydrophobic bond interactions. These findings highlight C. cassia as a promising source of natural anti-obesity agents.
Open AccessIdentification of an Inhibitory Fraction from Cinnamomum cassia Against Digestive Lipases
Natural inhibitors of digestive lipases offer promising alternatives to conventional obesity medications. This study screened nine medicinal plant extracts, identifying the ethanolic bark extract of Cinnamomum cassia as the most potent inhibitor for gastric and pancreatic lipases. Using an integrated approach combining bioactivity-guided fractionation and mass spectrometry, we isolated the highly active fraction, F3-1-1, which exhibited dose- and time-dependent inhibitory effects against human and porcine pancreatic lipases, as well as dog gastric lipase (DGL). Further mass spectrometry and peptide mass fingerprint analysis putatively annotated cinncassiol A-19 glucoside as a bioactive constituent. Notably, this compound was likely bound covalently to the catalytic peptide containing the Ser153 residue in DGL, characterized by a mass shift of +553.10 Da. Molecular docking simulations supported these suggestions, demonstrating stable interactions within the catalytic pocket of DGL through hydrogen and hydrophobic bond interactions. These findings highlight C. cassia as a promising source of natural anti-obesity agents.
- Open Access
- 24 August 2026
- Published by MDPI AG in Preprints.org
Cinncassiol A-19 Glucoside from Cinnamomum cassia Targets Digestive Lipases Through Covalent Inhibition: A Promising Natural Strategy Against Obesity
Natural inhibitors of digestive lipases offer promising alternatives to conventional obesity medications. This study screened nine medicinal plant extracts identifying the ethanolic bark extract of Cinnamomum cassia as the most potent inhibitor for gastric and pancreatic lipases. Using an integrated approach combining bioactivity-guided fractionation and mass spectrometry, we isolated the highly active fraction, F3-1-1, which exhibited dose- and time-dependent inhibitory effects against human and porcine pancreatic lipases, as well as dog gastric lipase (DGL). Further mass spectrometry and peptide mass fingerprint analysis identified cinncassiol A-19 glucoside as the main bioactive constituent. Notably, this compound forms covalent complexes with the catalytic peptide containing the Ser153 residue in DGL, characterized by a mass shift of +553.10 Da. Molecular docking simulations supported these results, demonstrating stable interactions within the catalytic pocket of DGL through hydrogen and hydrophobic bond interactions. These findings highlight C. cassia as a promising source of natural anti-obesity agents.
- 24 August 2026
- Published by MDPI AG in Preprints.org
Open AccessCinncassiol A-19 Glucoside from Cinnamomum cassia Targets Digestive Lipases Through Covalent Inhibition: A Promising Natural Strategy Against Obesity
Natural inhibitors of digestive lipases offer promising alternatives to conventional obesity medications. This study screened nine medicinal plant extracts identifying the ethanolic bark extract of Cinnamomum cassia as the most potent inhibitor for gastric and pancreatic lipases. Using an integrated approach combining bioactivity-guided fractionation and mass spectrometry, we isolated the highly active fraction, F3-1-1, which exhibited dose- and time-dependent inhibitory effects against human and porcine pancreatic lipases, as well as dog gastric lipase (DGL). Further mass spectrometry and peptide mass fingerprint analysis identified cinncassiol A-19 glucoside as the main bioactive constituent. Notably, this compound forms covalent complexes with the catalytic peptide containing the Ser153 residue in DGL, characterized by a mass shift of +553.10 Da. Molecular docking simulations supported these results, demonstrating stable interactions within the catalytic pocket of DGL through hydrogen and hydrophobic bond interactions. These findings highlight C. cassia as a promising source of natural anti-obesity agents.