Phytochemical Phenolic Profile, Cholinesterase and α-Glucosidase Inhibitory Activities Rationalized by Molecular Docking, and Antioxidant Capacity of Hibiscus sabdariffa.
7 affiliations
- 1Green Biotechnologies Research Centre, School of Agricultural and Environmental Sciences, University of Limpopo, Private Bag X1106, Sovenga 0727, South Africa.
- 2Dogubayazit Ahmed-i Hani Vocational School, Agri Ibrahim Cecen University, Agri 04400, Türkiye.
- 3Central Researching Laboratory, Agri Ibrahim Cecen University, Agri 04100, Türkiye.
- 4Department of Chemistry, Faculty of Science and Art, Erzincan Binali Yıldırım University, Erzincan 24100, Türkiye.
- 5Department of Food Technology, Technical Sciences Vocational School, Atatürk University, Erzurum 25030, Türkiye.
- 6Department of Bioengineering, Faculty of Engineering, Bilecik Şeyh Edebali University, Bilecik 11230, Türkiye.
- 7Department of Biochemistry, Faculty of Pharmacy, Agrı Ibrahim Cecen University, Agri 04100, Türkiye.
Abstract
This study aimed to evaluate the antioxidant, anticholinesterase, and α-glucosidase (AG) inhibitory activities of the ethanolic leaf extract, characterize its phenolic composition, and investigate the interactions of the major identified phytochemicals with the target enzymes through molecular docking analysis. The phenolic profile was determined by LC-MS/MS, antioxidant activity was assessed using DPPH and ABTS radical scavenging assays, enzyme inhibitory activities against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and AG were evaluated in vitro, and molecular docking was performed to examine ligand-enzyme interactions. Among the analyzed compounds, quercetin, myricetin, fumaric acid, vanillic acid, 4-hydroxybenzoic acid, and salicylic acid were identified as the predominant phenolics in the leaf extract. The extract exhibited DPPH and ABTS radical scavenging activities of approximately 19% and 11%, respectively. It also demonstrated potent enzyme inhibitory activity, with IC₅₀ values of 5.76 ± 0.21 µg/mL for AChE, 3.82 ± 0.17 µg/mL for BChE, and 6.24 ± 0.50 µg/mL for AG. Molecular docking analysis revealed that myricetin and quercetin exhibited the most favorable binding affinities toward AChE, BChE, and AG. Myricetin showed docking scores of -11.188, -9.642, and -7.899 kcal/mol against AChE, BChE, and AG, respectively, supported by hydrogen-bonding, π-π stacking, and hydrophobic interactions within the enzyme active sites. Re-docking validation yielded RMSD values below 2.0 Å for all targets, confirming the reliability of the docking protocol. These findings demonstrate that H. sabdariffa leaf extract is a rich source of bioactive phenolics with promising antioxidant and enzyme inhibitory properties, while molecular docking provides structural evidence supporting the observed biological activities.
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BibTeX
@article{ndhlala2026phytochemical,
title = {{Phytochemical Phenolic Profile, Cholinesterase and α-Glucosidase Inhibitory Activities Rationalized by Molecular Docking, and Antioxidant Capacity of Hibiscus sabdariffa.}},
author = {Ashwell Rungano Ndhlala and Emrah Dikici and Sevgi Altın and Arzu Kavaz Yüksel and Mesut Işık and Ahmet Gokhan Aggul and Ekrem Köksal},
journal = {Molecules (Basel, Switzerland)},
year = {2026},
month = sep,
doi = {10.3390/molecules31193374},
url = {https://europepmc.org/article/MED/42883142},
note = {CC BY},
}
RIS
TY - JOUR
TI - Phytochemical Phenolic Profile, Cholinesterase and α-Glucosidase Inhibitory Activities Rationalized by Molecular Docking, and Antioxidant Capacity of Hibiscus sabdariffa.
AU - Ashwell Rungano Ndhlala
AU - Emrah Dikici
AU - Sevgi Altın
AU - Arzu Kavaz Yüksel
AU - Mesut Işık
AU - Ahmet Gokhan Aggul
AU - Ekrem Köksal
PY - 2026
DA - 2026/09/23
JO - Molecules (Basel, Switzerland)
DO - 10.3390/molecules31193374
UR - https://europepmc.org/article/MED/42883142
AB - This study aimed to evaluate the antioxidant, anticholinesterase, and α-glucosidase (AG) inhibitory activities of the ethanolic leaf extract, characterize its phenolic composition, and investigate the interactions of the major identified phytochemicals with the target enzymes through molecular docking analysis. The phenolic profile was determined by LC-MS/MS, antioxidant activity was assessed using DPPH and ABTS radical scavenging assays, enzyme inhibitory activities against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and AG were evaluated in vitro, and molecular docking was performed to examine ligand-enzyme interactions. Among the analyzed compounds, quercetin, myricetin, fumaric acid, vanillic acid, 4-hydroxybenzoic acid, and salicylic acid were identified as the predominant phenolics in the leaf extract. The extract exhibited DPPH and ABTS radical scavenging activities of approximately 19% and 11%, respectively. It also demonstrated potent enzyme inhibitory activity, with IC₅₀ values of 5.76 ± 0.21 µg/mL for AChE, 3.82 ± 0.17 µg/mL for BChE, and 6.24 ± 0.50 µg/mL for AG. Molecular docking analysis revealed that myricetin and quercetin exhibited the most favorable binding affinities toward AChE, BChE, and AG. Myricetin showed docking scores of -11.188, -9.642, and -7.899 kcal/mol against AChE, BChE, and AG, respectively, supported by hydrogen-bonding, π-π stacking, and hydrophobic interactions within the enzyme active sites. Re-docking validation yielded RMSD values below 2.0 Å for all targets, confirming the reliability of the docking protocol. These findings demonstrate that H. sabdariffa leaf extract is a rich source of bioactive phenolics with promising antioxidant and enzyme inhibitory properties, while molecular docking provides structural evidence supporting the observed biological activities.
SN - 1420-3049
ER -