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Current Computer-Aided Drug Design

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ISSN (Print): 1573-4099
ISSN (Online): 1875-6697

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Research Article

Exploration of Diosmin to Control Diabetes and Its Complications-an In Vitro and In Silico Approach

Author(s): Kushagra Dubey*, Raghvendra Dubey, Revathi Gupta and Arun Gupta

Volume 17, Issue 2, 2021

Published on: 24 March, 2020

Page: [307 - 313] Pages: 7

DOI: 10.2174/1573409916666200324135734

Price: $65

Abstract

Background: Diosmin is a flavonoid obtained from the citrus fruits of the plants. Diosmin has blood lipid lowering activities, antioxidant activity, enhances venous tone and microcirculation, protects capillaries, mainly by reducing systemic oxidative stress.

Objective: The present study demonstrates the potential of Diosmin against the enzymes aldose reductase, α-glucosidase, and α-amylase involved in diabetes and its complications by in vitro evaluation and reverse molecular docking studies.

Methods: The assay of aldose reductase was performed by using NADPH as starting material and DL-Glyceraldehyde as a substrate. DNS method was used for alpha amylase inhibition and in alpha glucosidase inhibitory activity p-nitrophenyl glucopyranoside (pNPG) was used as substrate. The reverse molecular docking studies was performed by using Molegro software (MVD) with grid resolution of 30 Å.

Results: Diosmin shows potent inhibitory effect against aldose reductase (IC50:333.88±0.04 μg/mL), α-glucosidase (IC50:410.3±0.01 μg/mL) and α-amylase (IC50: 404.22±0.02 μg/mL) respectively. The standard drugs shows moderate inhibitory activity for enzymes. The MolDock Score of Diosmin was -224.127 against aldose reductase, -168.17 against α-glucosidase and - 176.013 against α-amylase respectively, which was much higher than standard drugs.

Conclusion: From the result it was concluded that diosmin was a potentially inhibitor of aldose reductase, alpha amylase and alpha glucosidase enzymes then the standard drugs and it will be helpful in the management of diabetes and its complications. This will also be benevolent to decrease the socio economical burden on the middle class family of the society.

Keywords: Reverse docking, aldose reductase, α -glucosidase, α -amylase, diosmin, p-nitrophenyl glucopyranoside.

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[1]
Maritim, A.C.; Sanders, R.A.; Watkins, J.B. III Diabetes, oxidative stress, and antioxidants: a review. J. Biochem. Mol. Toxicol., 2003, 17(1), 24-38.
[http://dx.doi.org/10.1002/jbt.10058] [PMID: 12616644]
[2]
Papatheodorou, K.; Banach, M.; Bekiari, E. Editorial Complications of Diabetes 2017. J. Diabetes Res., 2018, 2018, 10.
[http://dx.doi.org/10.1155/2018/3086167]
[3]
Kumar, S.; Kumar, V.; Rana, M.; Kumar, D. Enzymes Inhibitors From Plants: An Alternate Approach To Treat Diabetes. Pharmacogn. Commun., 2012, 2, 18.
[http://dx.doi.org/10.5530/pc.2012.2.4]
[4]
Nair, S.S.; Kavrekar, V.; Mishra, A. In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts. Eur. J. Exp. Biol., 2013, 3, 128.
[5]
Moein, S.; Pimoradloo, E.; Moein, M.; Vessal, M. Evaluation of Antioxidant Potentials and α-Amylase Inhibition of Different Fractions of Labiatae Plants Extracts: As a Model of Antidiabetic Compounds Properties. BioMed Res. Int., 2017.20177319504
[http://dx.doi.org/10.1155/2017/7319504] [PMID: 29082253]
[6]
Li, Y.Q.; Zhou, F.C.; Gao, F.; Bian, J.S.; Shan, F. Comparative evaluation of quercetin, isoquercetin and rutin as inhibitors of α-glucosidase. J. Agric. Food Chem., 2009, 57(24), 11463-11468.
[http://dx.doi.org/10.1021/jf903083h] [PMID: 19938837]
[7]
Proença, C.; Freitas, M.; Ribeiro, D.; Oliveira, E.F.T.; Sousa, J.L.C.; Tomé, S.M.; Ramos, M.J.; Silva, A.M.S.; Fernandes, P.A.; Fernandes, E. α-Glucosidase inhibition by flavonoids: an in vitro and in silico structure-activity relationship study. J. Enzyme Inhib. Med. Chem., 2017, 32(1), 1216-1228.
[http://dx.doi.org/10.1080/14756366.2017.1368503] [PMID: 28933564]
[8]
Lee, S.J.; Park, W.H.; Park, S.D.; Moon, H.I. Aldose reductase inhibitors from Litchi chinensis Sonn. J. Enzyme Inhib. Med. Chem., 2009, 24(4), 957-959.
[http://dx.doi.org/10.1080/14756360802560867] [PMID: 19555177]
[9]
Alim, Z.; Kilinç, N.; Şengül, B.; Beydemir, Ş. Inhibition behaviours of some phenolic acids on rat kidney aldose reductase enzyme: an in vitro study. J. Enzyme Inhib. Med. Chem., 2017, 32(1), 277-284.
[http://dx.doi.org/10.1080/14756366.2016.1250752] [PMID: 28111996]
[10]
Ghosh, S.; More, P.; Derle, A.; Patil, A.B.; Markad, P.; Asok, A.; Kumbhar, N.; Shaikh, M.L.; Ramanamurthy, B.; Shinde, V.S.; Dhavale, D.D.; Chopade, B.A. Diosgenin from Dioscorea bulbifera: novel hit for treatment of type II diabetes mellitus with inhibitory activity against α-amylase and α-glucosidase. PLoS One, 2014, 9(9)e106039
[http://dx.doi.org/10.1371/journal.pone.0106039] [PMID: 25216353]
[11]
Kalita, D.; Holm, D.G.; LaBarbera, D.V.; Petrash, J.M.; Jayanty, S.S. Inhibition of α-glucosidase, α-amylase, and aldose reductase by potato polyphenolic compounds. PLoS One, 2018, 13(1)e0191025
[http://dx.doi.org/10.1371/journal.pone.0191025] [PMID: 29370193]
[12]
Grinter, S.Z.; Liang, Y.; Huang, S.Y.; Hyder, S.M.; Zou, X. An inverse docking approach for identifying new potential anti-cancer targets. J. Mol. Graph. Model., 2011, 29(6), 795-799.
[http://dx.doi.org/10.1016/j.jmgm.2011.01.002] [PMID: 21315634]
[13]
Luo, Q.; Zhao, L.; Hu, J.; Jin, H.; Liu, Z.; Zhang, L. The scoring bias in reverse docking and the score normalization strategy to improve success rate of target fishing. PLoS One, 2017, 12(2)e0171433
[http://dx.doi.org/10.1371/journal.pone.0171433] [PMID: 28196116]
[14]
Furlan, V.; Konc, J.; Bren, U. Inverse molecular docking as a novel approach to study anticarcinogenic and anti-neuroinflammatory effects of curcumin. Molecules, 2018, 23(12), 1.
[http://dx.doi.org/10.3390/molecules23123351] [PMID: 30567342]
[15]
Shalkami, A.S.; Hassan, M.; Bakr, A.G. Anti-inflammatory, antioxidant and anti-apoptotic activity of diosmin in acetic acid-induced ulcerative colitis. Hum. Exp. Toxicol., 2018, 37(1), 78-86.
[http://dx.doi.org/10.1177/0960327117694075] [PMID: 29187079]
[16]
Ajani, E.O.; Sabiu, S.; Odufuwa, K.T. Evaluation of Lens Aldose Reductase Inhibitory and Free Radical Scavenging Potential of Fractions of Lonchocarpus cyanescens : Potential for Cataract Remediation. Pharmacogn. J., 2017, 9, 62.
[http://dx.doi.org/10.5530/pj.2017.1.12]
[17]
Patel, D.K.; Kumar, R.; Sairam, K.; Hemalatha, S. Aldose reductase inhibitory activity of alcoholic extract of Pedalium murex Linn fruit. Asian Pac. J. Trop. Biomed., 2012, 2, S265.
[http://dx.doi.org/10.1016/S2221-1691(12)60172-5]
[18]
Ahmed, S.; Al-Rehaily, A.J.; Alam, P.; Alqahtani, A.S.; Hidayatullah, S.; Rehman, M.T.; Mothana, R.A.; Abbas, S.S.; Khan, M.U.; Khalid, J.M.; Siddiqui, N.A. Antidiabetic, antioxidant, molecular docking and HPTLC analysis of miquelianin isolated from Euphorbia schimperi C. Presl. Saudi Pharm. J., 2019, 27(5), 655-663.
[http://dx.doi.org/10.1016/j.jsps.2019.03.008] [PMID: 31297020]
[19]
Madhuri, M.; Prasad, C.; Rao Avupati, V. In silico Protein-Ligand Docking Studies on thiazolidinediones as potential Anticancer Agnets. Int. J. Comput. Appl., 2014, 95, 13.
[20]
Heble, NK Molecular docking studies of phytoconstituents identifies in Crocus sativus, curcuma longa, cassia occidentalis and Moringa oleifera on thymidylate synthase- An enyme target for anti-cancer activity. J. Appl. Pharm. Sci., 2016, 6, 131.
[http://dx.doi.org/10.7324/JAPS.2016.601218]
[21]
Mavillapalli, R.C.; Jeyabalan, S.; Muthusamy, S.K. molecular docking studies of phyoconstituents identified in cinnamomum verum and coriandrum sativum on HMG COA Reductase- an enzyme target for Antihyperlipidemic Activity. Int. J. Pharm. Sci. Res., 2017, 8, 4172.

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