Exploring Ctenolepis garcinii as a natural anti-diabetic agent: A phytochemical, biochemical and molecular docking approach
Paper Details
Exploring Ctenolepis garcinii as a natural anti-diabetic agent: A phytochemical, biochemical and molecular docking approach
Abstract
Diabetes mellitus is a major global health challenge, and plant-derived bioactive compounds offer promising therapeutic alternatives. Ctenolepis garcinii is traditionally used in ethnomedicine, but its anti-diabetic potential has not been systematically validated. This study aimed to evaluate the physicochemical parameters, phytochemical constituents, fluorescence characteristics, flavonoid profiling, in vitro α-amylase inhibitory activity, and molecular docking interactions of Ctenolepis garcinii. Physicochemical analysis included determination of moisture content, ash values, and extractive values. Quantitative phytochemical screening measured flavonoids, alkaloids, tannins, saponins, phenols, crude fiber, ash, and pectic substances. Fluorescence analysis of powdered samples was performed using chemical reagents under visible and UV light. Thin Layer Chromatography (TLC) identified flavonoids using quercetin and rutin as standards. In vitro α-amylase inhibitory activity was assessed by the DNSA method at concentrations 100–500 µg/ml, with acarbose as standard. Molecular docking was conducted to evaluate the binding affinity of rutin with human pancreatic α-amylase (PDB: 1B2Y). Physicochemical analysis showed moisture content 1.97% and total ash 32%, reflecting mineral richness. Phytochemical screening revealed high amounts of tannins (32.4%), pectic substances (23.8%), saponins (16.5%), and flavonoids (10.2%). Fluorescence analysis provided distinct diagnostic features under different reagents. TLC confirmed the presence of flavonoids with Rf values comparable to quercetin (0.85) and rutin (0.65). In vitro α-amylase inhibition was dose-dependent, with 87.0 ± 2.10% inhibition at 500 µg/ml, nearly equivalent to acarbose (92.41 ± 0.81%). Molecular docking showed rutin exhibited strong binding affinity (-8.80 kcal/mol) with α-amylase, forming interactions with critical residues (Gly306, His305, Tyr151, Asp300, etc.). Ctenolepis garcinii exhibits significant anti-diabetic potential, attributable to its rich flavonoid and tannin content. The combination of in vitro and in silico findings supports its inhibitory effect on carbohydrate-hydrolyzing enzymes, validating its ethnomedicinal use. Further in vivo and clinical studies are recommended to establish its therapeutic efficacy and safety.
Ali H, Houghton PJ, Soumyanath A. 2006. α-amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amarus. Journal of Ethnopharmacology 107(3), 449–455. https://doi.org/10.1016/j.jep.2006.03.013
Harborne JB. 1998. Phytochemical methods: A guide to modern techniques of plant analysis. Springer. https://doi.org/10.1007/978-94-009-5570-7
Bailey CJ. 2015. Metformin: Historical overview. Diabetologia 60(9), 1566–1576. https://doi.org/10.1007/s00125-015-3642-7
Bernfeld P. 1955. Amylases, α and β. In: Colowick SP, Kaplan NO (eds.). Methods in Enzymology 1, 149–158. Academic Press. https://doi.org/10.1016/0076-6879(55)01021-5
Ghasemzadeh A, Ghasemzadeh N. 2011. Flavonoids and phenolic acids: Role and biochemical activity in plants and human health. The Scientific World Journal 2011, 1–9. https://doi.org/10.1100/tsw.2011.702
International Diabetes Federation. 2021. IDF diabetes atlas, 10th edition. International Diabetes Federation, Brussels, Belgium.
Kokate CK. 2005. Practical pharmacognosy. Vallabh Prakashan.
Kokoshi CJ, Kokoshi RJ, Sharma FJ. 1958. Fluorescence of powdered vegetable drugs under UV radiation. Journal of the American Pharmaceutical Association 47(10), 715–717. https://doi.org/10.1002/jps.3030471038
Kumar S, Pandey AK. 2012. Chemistry and biological activities of flavonoids: An overview. The Scientific World Journal 2013, 162750. https://doi.org/10.1155/2013/162750
Lo Piparo E, Scheib H, Frei N, Williamson G, Grigorov M, Chou CJ. 2008. Flavonoids for controlling starch digestion: Structural requirements for inhibiting human α-amylase. Journal of Medicinal Chemistry 51(12), 3555–3561. https://doi.org/10.1021/jm800115x
Patel DK, Prasad SK, Kumar R, Hemalatha S. 2012. An overview on antidiabetic medicinal plants having insulin mimetic property. Asian Pacific Journal of Tropical Biomedicine 2(4), 320–330. https://doi.org/10.1016/S2221-1691(12)60032-X
Sales PM, Souza PM, Simeoni LA, Magalhães PO, Silveira D. 2012. α-amylase inhibitors: A review of raw material and isolated compounds from plant source. Journal of Pharmacy & Pharmaceutical Sciences 15(1), 141–183. https://doi.org/10.18433/j3nc79
Sharma PC, Yelne MB, Dennis TJ. 2011. Database on medicinal plants used in Ayurveda. Central Council for Research in Ayurveda and Siddha.
Tadera K, Minami Y, Takamatsu K, Matsuoka T. 2006. Inhibition of α-glucosidase and α-amylase by flavonoids. Journal of Nutritional Science and Vitaminology 52(2), 149–153. https://doi.org/10.3177/jnsv.52.149
Trease GE, Evans WC. 2002. Pharmacognosy. Saunders.
Trott O, Olson AJ. 2010. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry 31(2), 455–461. https://doi.org/10.1002/jcc.21334
Wagner H, Bladt S. 1996. Plant drug analysis: A thin layer chromatography atlas. Springer. https://doi.org/10.1007/978-3-642-00574-9
World Health Organization. 1998. Quality control methods for medicinal plant materials. WHO.
A. M. Thafshila Aafrin, R. Anuradha, 2025. Exploring Ctenolepis garcinii as a natural anti-diabetic agent: A phytochemical, biochemical and molecular docking approach. Int. J. Biosci., 27(4), 208-214.
Copyright © 2025 by the Authors. This article is an open access article and distributed under the terms and conditions of the Creative Commons Attribution 4.0 (CC BY 4.0) license.


