Characterization and Evaluation of Vernonia amygdalina Extracts for its Antidiabetic Potentials

Characterization and Evaluation of Vernonia amygdalina Extracts for its Antidiabetic Potentials

Loading document ...
Page
of
Loading page ...

Author(s)

Author(s): Adewole Ezekiel, Ojo A, Ogunmodede O.T, Adewumi D.F, Omoaghe A.O, Jamshed I

Download Full PDF Read Complete Article

DOI: 10.18483/ijSci.1462 185 539 31-38 Volume 7 - Jan 2018

Abstract

Background: There is increase in the demand for the use of medicinal plants for the treatment of various ailments such as cancer, hypertension and diabetes locally as a result of the inability of the synthesized drugs to completely eradicate the ailments and also with the attendant side effects attached to the use of drugs. Objective: The aim of this research work was to investigate the Aldose reductase, α-glucosidase, β -glucosidase and maltase glucoamylase inhibitory potential of the crude extracts of Vernonia amygdalina, and characterizing the extracts. Materials and method: The leaves of the plant was obtained, air dried and turned to powdered form using commercial grinding machine with dimension 34×38×75. The extracted crudes were subjected into in-vitro studies of the inhibitory potentials using recommended protocols. The IC50 values were calculated using Graph pad prism 5.0 software and the identified compounds were screened for drug properties using ONLINE OSIRIS server explorer. Results: The (IC50 0.6 ± 0.03 μg/mL) of the chloroform extract was better than the methanolic extract of IC50 (1.532±0.63μg/mL) and the results were better than the acarbose standard (IC50 234.6 + 2.01μM). The maltase glucoamylase inhibitory potentials of the chloroform and methanolic extracts in the range of IC50 1.112 ± 0.90 μg/mL and 1.315 ± 0.7 μg/mL. The β-glucosidase screening of the extracts results indicated that they do not have good selective inhibitor properties. IC50 of Aldose reductase (ALR2) of chloroform extract IC50 (1.339+0.264μg/mL) was better than that of methanolic extract of IC50 (1.437+0.6μg/mL) and these values were better when compared with the standard, sorbinil of IC50 (3.10 +0.20μM).The aldehyde reductase (ALR1) of methanolic extract IC50 (0.325+0.02μg/mL) was better than that of chloroform extract of IC50 (0.964+0.16μg/mL) and when compared with standard 10mM vaproic acid IC50 (57.4 +10μM).The GC-MS of the chloroform extract revealed compounds which were screened computationally to for various drug properties such as drug likeness, cLogS, cLogP, H-bond acceptor and H-bond Donor. Conclusion: The promising inhibitory potential of the plant extracts and characterization of the extract is an indication of the usefulness of the plant for the treatment of diabetes.

Keywords

Diabetes mellitus, drug properties, aldose reductase, α-glucosidase, maltase glucoamylase, β-glucosidase

References

  1. G. Kaushik, S. Satya, R. K. Khandelwal and S. N. Naik (2010); commonly consumed Indian plant food materials in the management of diabetes mellitus, Diabetes & Metabolic Syndrome: Clinical Research & Reviews. Volume 4, pg 21-40.
  2. S. Cheplick, Y. I. Kwon, P. Bhowmik and K. Shetty (2010). Phenolic-linked variation in strawberry cultivars for potential dietary management of hyperglycemia and related complications of hypertension, Bioresour. Technol. 101, 404-413.
  3. W.L. Li, H.C. Zheng, J. Bukuru, N. De Kimpe (2004). ‘Natural medicines used in the traditional Chinese medical system for therapy of diabetes mellitus’ Journal of Ethnopharmacology 92 pg 1–21 (a review)
  4. www. Wikipedia.org// α-glucosidase inhibitor
  5. Quezada-Calvillo R, Sim L, Ao Z, Hamaker BR, Quaroni A, Brayer GD, Sterchi EE, Robayo-Torres CC, Rose DR, Nichols BL (2008). "Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit". J. Nutr. 138 (4): 685–92. PMID 1835632
  6. Grundy, S. M., Benjamin, I. J., Burke, G. L., Chait, A., Eckel, R. H., Howard, B. V., ... Sowers, J. R. (1999). Diabetes and cardiovascular disease: A statement for healthcare professionals from the american heart association. Circulation, 100(10), 1134-1146 [7] P. Fresneau, M. Cussac, J.-M. Morand, B. Szymonski, D. Tranqui and G. Leclerc, (1998); J. Med. Chem., 41 (24), 4706‒ 4715
  7. Robinson Jr WG.., Nagata M, Kinoshita JH. Aldose reductase and retinal capillary basement membrane thickening. Experimental Eye Research. Volume 46, Issue 3, March 1988, Pages 343-348
  8. Tomlinson, D. R., Willars G. B. and Carrington, A. L. (1992). Aldose reductase inhibitors and diabetic complications. Pharmacol. Ther., 54(2), 151‒199.
  9. Herbal medicine--its use in treating some symptoms of AIDS; 9th International AIDS Conference.
  10. Report: Indigenous Approached to the HIV/AIDS Scourge in Uganda, chapter 5, archived September 28, 2007 at the Wayback Medicine.
  11. Traditional Medicine Development for Medical and Dental Primary Health Care delivery system in Africa’, African Journal of Traditional Complementary and Alternative Medicines.Volume 2, issue 1, 2005, pages 46-61.
  12. Udoamaka F. Ezuruike and Jose M. Prieto (2014). ‘The use of plants in the traditional management of diabetes in Nigeria, Pharmacological and toxicological considerations’ Journal of Ethnopharmacology, volume 155, issue 2, pg:857–924.
  13. Akah, P.A., and Okafor,C.L.,(1992). ‘Blood sugar lowering effect of Vernonia amygdalina Del, in an experimental rabbit model’.Phytotherapy Research volume 6, pg 171–173.
  14. Ong, K.W.,Hsu,A.,Song,L.,Huang,D.,Tan,B.K.H.,(2011). ‘Polyphenols-rich Vernonia amygdalina shows anti-diabetic effects in streptozotocin-induced diabetic rats’. Journal ofEthnopharmacology volume 133,pg 598–607.
  15. Ejike,C.E.C.C.,Awazie,S.O.,Nwangozi,P.A., and Godwin,C.D.,(2013). ‘Synergisticpost- prandial blood glucose modulatory properties of Vernonia amygdalina (Del.), Gongronema latifolium (Benth.) and Occimum gratissimum (Linn.) aqueous decoctions. Journal of Ethnopharmacology, volume 149,pg 111–116.
  16. Hayman, S. and Kinoshita, J. H. (1965); ‘Isolation and properties of lens aldose reductase’, J. Biol. Chem., 240, 877-82.
  17. Ward, W. H. J., Sennitt, C. M., Ross, H., Dingle, A., Tinms, D., Mirrlees, D. J., and Tuffin, D. P., (1990); ‘Ponalrestat: a potent and specific inhibitor of aldose reductase’, Biochem. Pharmacol., 39: 337.
  18. H. Y. Ma, H. Y. Gao, L. Sun, J. Huang, X. M. Xu and L. J. Wu (2011); ‘constituents with alpha-glucosidase and advanced glycation end-product formation inhibitory activities from Salvia miltiorrhiza’ Bge, J. Nat. Med. 65, 37-42.
  19. M. Pérez, F. J. Muñoz, E. Muñoz, M. Fernández, J. V. Sinisterra and M. J. Hernáiz (2008); ‘Synthesis of novel glycoconjugates and evaluation as inhibitors against β-glucosidase from almond’, J. Mol. Catal. B: Enzym. 52–53, 153-157.
  20. Lee LMY, Salvatore AK, Flanagan PR, Forstner GG. Isolation of a Detergent-Solubilized Maltase/Glucoamylase from Rat Intestine and its Comparison with a Maltase/Glucoamylase solubilized by Papain. Biochem J 1980;187:437-446.
  21. Flanagan PR, Forstner GG. Purification of Rat Intestinal Maltase/Glucoamylase and its Anomalous Dissociation either by Heat or by Low pH. Biochem J 1978;173:553-563.
  22. Tanaka A, Ohya M, Yammato T, Nakagawa C, Tsuji T, Senoo K, Obata H, Steady-State Inhibitory Kinetics Studies on the Ligand Binding Modes of Aspergillus niger Glucoamylase. Biosci Biotechnol Biochem 1999;63:1548-1552.
  23. D. Rakowitz, R. Maccari, R. Ottana and M. G.(2006); ‘Vigorita, Bioorg. Med. Chem., 14, 567–574; (b) S. Ali, A. Saeed, N. Abbas, M. Shahid, M. Bolte and J, (2012); Iqbal, Med. Chem. Commun., 2012, 3, 1428–1434.
  24. Rammohan Subramanian, M. Zaini Asmawi and Amirin Sadikun (2008). ‘In vitro α-glucosidase and α-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide’Acta Biochimica Polonica, volume 55, No: 2, pg:391-398
  25. Sindhu. S. Nair, Vaibhavi Kavrekar and Anshu Mishra (2013). ‘In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts’ European Journal of Experimental Biology, volume 3(1):128-132.
  26. R.M. Balaji, Chitra Jeyaram, K. Meenakshi , Sundaram and M.S. Ramasamy, (2015). ‘Studies on Antidiabetic Activity of Indian Medicinal Plants Using –Amylase and -Glucosidase Inhibitory Activity - A Pathway to Antidiabetic Drugs’World Journal of Medical Sciences 12 (3): 207-212.
  27. N. Verma, B. C. Behera and B. O. Sharma (2012); ‘Glucosidase inhibitory and radical scavenging properties of lichen metabolites salazinic acid, sekikaic acid and usnic acid’. Hacett. J. Biol. Chem. 40, 7–21.
  28. T. Sander, OSIRIS property explorer. Allschwil: Actelion Pharmaceuticals Ltd 2001.

Cite this Article:

International Journal of Sciences is Open Access Journal.
This article is licensed under a Creative Commons Attribution 4.0 International (CC BY 4.0) License.
Author(s) retain the copyrights of this article, though, publication rights are with Alkhaer Publications.

Search Articles

Issue June 2023

Volume 12, June 2023


Table of Contents



World-wide Delivery is FREE

Share this Issue with Friends:


Submit your Paper