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Current Enzyme Inhibition

Editor-in-Chief

ISSN (Print): 1573-4080
ISSN (Online): 1875-6662

Research Article

Antioxidant Activity and Inhibitory Effect of Curcumin on Some Enzymes Involved in Several Diseases: Acetylcholinesterase, Butyrylcholinesterase, α-glucosidase and Tyrosinase

Author(s): Seghira Bisset, Widad Sobhi*, Chawki Bensouici and Abdelhalim khenchouche

Volume 18, Issue 3, 2022

Published on: 10 August, 2022

Page: [172 - 179] Pages: 8

DOI: 10.2174/1573408018666220602091615

Price: $65

Abstract

Aim: This study investigates the potential effect of pure curcumin on the inhibition of different enzymes involved in several diseases.

Background: Several chronic diseases such as Alzheimer’s, diabetes, and Parkinson’s are related to oxidative stress and enzyme activity. Today, various plant origin products are beneficial against several chronic diseases with secondary metabolites such as phenolic compounds. Curcumin, a polyphenol yellow- orange pigment in turmeric spices, has a wide range of biological activities with quite a safety.

Objective: This study aimed to investigate the antioxidant and inhibitory potential against key enzymes involved in human pathology, namely Alzheimer's disease (Acetylcholinesterase (AChE), and Butyrylcholinesterase (BChE)), diabetes (α-glucosidase), hyperpigmentation and Parkinson’s diseases (Tyrosinase) of curcumin.

Methods: 1,1-diphenyl-2-picrylhydrazyl free radical (DPPH●) and hydrogen peroxide radicals (H2O2) assays were used to evaluate the antioxidant capacity of curcumin, and enzyme inhibitory activity was evaluated using in vitro standard procedures.

Results: Curcumin exhibited an excellent antioxidant effect with an IC50 value significantly less than Vit C reference. In enzyme inhibitory activity, curcumin demonstrated excellent inhibitory activity against AChE, BChE and α-glucosidase. The finding showed that curcumin was significantly less than the reference galantamine against AChE but more than the references galantamine and acarbose against BChE and α-glucosidase, respectively. Whereas for anti-tyrosinase activity, curcumin displayed weak inhibitory activity compared with the standard inhibitor, Kojic acid.

Conclusion: These results indicated that curcumin showed promising antioxidant, anti-Alzheimer, and anti-diabetic properties and might be used as potential natural drugs against these diseases.

Keywords: Curcumin, oxidative stress, acetylcholinesterase, butyrylcholinesterase, α-glucosidase, tyrosinase.

Graphical Abstract
[1]
Aggarwal BB, Kumar A, Bharti AC. Anticancer potential of curcumin: Preclinical and clinical studies. Anticancer Res 2003; 23(1A): 363-98.
[PMID: 12680238]
[2]
Rathore S, Mukim M, Sharma P, Devi S, Nagar JC, Khalid M. Curcumin: A review of its effects on human health. IJRR 2020; 7(1): 2454-37.
[3]
Mandal M, Jaiswal P, Mishra A. Role of curcumin and its nanoformulations in neurotherapeutics: A comprehensive review. J Biochem Mol Toxicol 2020; 34(6): e22478.
[http://dx.doi.org/10.1002/jbt.22478] [PMID: 32124518]
[4]
El-Desoky GE, Wabaidur SM, AlOthman ZA, Habila MA. Regulatory role of nano-curcumin against tartrazine-induced oxidative stress, apoptosis-related genes expression, and genotoxicity in rats. Molecules 2020; 25(24): 5801.
[http://dx.doi.org/10.3390/molecules25245801] [PMID: 33316931]
[5]
El-Desoky GE, Wabaidur SM, Habila MA, AlOthman ZA. Synergistic effects of curcumin and nano-curcumin against toxicity, carcinogen-icity, and oxidative stress induced by tartrazine at normal and cancer cell levels. Catalysts 2021; 11(10): 1203.
[http://dx.doi.org/10.3390/catal11101203]
[6]
Ouertani A, Neifar M, Ouertani R. Masmoudi, Amor Mosbah. Effectiveness of enzyme inhibitors in biomedicine and pharmacotherapy. Adv Tissue Eng Regen Med 2019; 5(2): 85-90.
[7]
Copeland RA, Harpel MR, Tummino PJ. Targeting enzyme inhibitors in drug discovery. Expert Opin Ther Targets 2007; 11(7): 967-78.
[http://dx.doi.org/10.1517/14728222.11.7.967] [PMID: 17614764]
[8]
Alothman ZA, Khan MR, Wabaidur SM, Siddiqui MR. Persistent organic pollutants: Overview of their extraction and estimation. Sens Lett 2012; 10(3-4): 698-704.
[http://dx.doi.org/10.1166/sl.2012.2344]
[9]
Bhowmick S, Saha A, AlFaris NA. et al. Structure-based identification of galectin-1 selective modulators in dietary food polyphenols: A pharmacoinformatics approach. Mol Divers 2021; 2121: 1-18.
[http://dx.doi.org/10.1007/s11030-021-10297-1] [PMID: 34482478]
[10]
Muthukutty B, Ganesamurthi J, Chen SM. et al. Construction of novel binary metal oxides: Copper oxide-tin oxide nanoparticles regulated for selective and nanomolar level electrochemical detection of anti-psychotic drug. Electrochim Acta 2021; 386: 138482.
[http://dx.doi.org/10.1016/j.electacta.2021.138482]
[11]
Gopi PK, Muthukutty B, Chen SM. et al. Platelet-structured strontium titanate perovskite decorated on graphene oxide as a nanocatalyst for electrochemical determination of neurotransmitter dopamine. New J Chem 2020; 44(42): 18431-41.
[http://dx.doi.org/10.1039/D0NJ03564E]
[12]
Asghari B, Zengin G, Bahadori MB, Abbas-Mohammadi M, Dinparast L. Amylase, glucosidase, tyrosinase, and cholinesterases inhibitory, antioxidant effects and GC-MS analysis of wild mint (Mentha longifolia var. calliantha) essential oil: A natural remedy. Eur J Integr Med 2018; 22: 44-9.
[http://dx.doi.org/10.1016/j.eujim.2018.08.004]
[13]
Majid H, Silva FVM. Inhibition of enzymes important for Alzheimer’s disease by antioxidant extracts prepared from 15 New Zealand medicinal trees and bushes. J R Soc N Z 2020; 50(4): 538-51.
[http://dx.doi.org/10.1080/03036758.2020.1741403]
[14]
You Q, Chen F, Wang X, Jiang Y, Lin S. Anti-diabetic activities of phenolic compounds in muscadine against alpha-glucosidase and pan-creatic lipase. Lebensm Wiss Technol 2012; 46(1): 164-8.
[http://dx.doi.org/10.1016/j.lwt.2011.10.011]
[15]
Wang KH, Lin RD, Hsu FL. et al. Cosmetic applications of selected traditional Chinese herbal medicines. J Ethnopharmacol 2006; 106(3): 353-9.
[http://dx.doi.org/10.1016/j.jep.2006.01.010] [PMID: 16497459]
[16]
Hasegawa T. Tyrosinase-expressing neuronal cell line as in vitro model of Parkinson’s disease. Int J Mol Sci 2010; 11(3): 1082-9.
[http://dx.doi.org/10.3390/ijms11031082] [PMID: 20480001]
[17]
Blois MS. Antioxidant determinations by the use of a stable free radical. Nature 1958; 4617(181): 1119-200.
[http://dx.doi.org/10.1038/1811199a0]
[18]
Ruch RJ, Cheng SJ, Klaunig JE. Prevention of cytotoxicity and inhibition of intercellular communication by antioxidant catechins isolated from Chinese green tea. Carcinogenesis 1989; 10(6): 1003-8.
[http://dx.doi.org/10.1093/carcin/10.6.1003] [PMID: 2470525]
[19]
Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 1961; 7(2): 88-95.
[http://dx.doi.org/10.1016/0006-2952(61)90145-9] [PMID: 13726518]
[20]
Lordan S, Smyth TJ, Soler-Vila A, Stanton C, Ross RP. The α-amylase and α-glucosidase inhibitory effects of Irish seaweed extracts. Food Chem 2013; 141(3): 2170-6.
[http://dx.doi.org/10.1016/j.foodchem.2013.04.123] [PMID: 23870944]
[21]
Deveci E, Tel-Çayan G, Duru ME. Phenolic profile, antioxidant, anticholinesterase and anti-tyrosinase activities of the various extracts of Ferula elaeochytris and Sideritis stricta. Int J Food Prop 2018; 21(1): 771-83.
[http://dx.doi.org/10.1080/10942912.2018.1431660]
[22]
Zhou K, Yu L. Effects of extraction solvent on wheat bran antioxidant activity estimation. Lebensm Wiss Technol 2004; 37(7): 717-21.
[http://dx.doi.org/10.1016/j.lwt.2004.02.008]
[23]
Moylan JS, Reid MB. Oxidative stress, chronic disease, and muscle wasting. Muscle Nerve 2007; 35(4): 411-29.
[http://dx.doi.org/10.1002/mus.20743] [PMID: 17266144]
[24]
Rafiquee MZA, Siddiqui MR, Haque HN. et al. Activation of molecular oxygen for the oxidation of 2-mercaptoethanol: A kinetic and mechanistic approach. J Ind Eng Chem 2016; 34: 84-8.
[http://dx.doi.org/10.1016/j.jiec.2015.10.039]
[25]
Khan T, Azad I, Ahmad R. et al. Molecular structure simulation of (E)-2-(butan-2-ylidene) hydrazinecarbothioamide using the DFT ap-proach, and antioxidant potential assessment of its complexes. J King Saud Univ Sci 2021; 33(2): 101313.
[http://dx.doi.org/10.1016/j.jksus.2020.101313]
[26]
Chen TW, Rajaji U, Chen SM. et al. Sonochemical preparation of carbon nanosheets supporting cuprous oxide architecture for high-performance and non-enzymatic electrochemical sensor in biological samples. Ultrason Sonochem 2020; 66: 105072.
[http://dx.doi.org/10.1016/j.ultsonch.2020.105072] [PMID: 32229388]
[27]
Dichi I, Breganó JW, Simão ANC, Cecchini R. Role of Oxidative Stress in Chronic Diseases. (1st ed.), Boca Raton: CRC Press 2014.
[http://dx.doi.org/10.1201/b16653]
[28]
Yeung AWK, Tzvetkov NT, Georgieva MG. et al. Reactive Oxygen Species (ROS) and their impact in neurodegenerative diseases: Litera-ture landscape analysis. Antioxid Redox Signal 2021; 34(5): 402-20.
[http://dx.doi.org/10.1089/ars.2019.7952] [PMID: 32030995]
[29]
Pazdro R, Burgess JR. The role of vitamin E and oxidative stress in diabetes complications. Mech Ageing Dev 2010; 131(4): 276-86.
[http://dx.doi.org/10.1016/j.mad.2010.03.005] [PMID: 20307566]
[30]
Zhang J, Hou X, Ahmad H, Zhang H, Zhang L, Wang T. Assessment of free radicals scavenging activity of seven natural pigments and protective effects in AAPH-challenged chicken erythrocytes. Food Chem 2014; 145: 57-65.
[http://dx.doi.org/10.1016/j.foodchem.2013.08.025] [PMID: 24128449]
[31]
Ozcelik B, Lee JH, Min DB. Effects of light, oxygen and pH on the 2,2- diphenyl-1-picrylhydrazyl (DPPH) method to evaluate antioxi-dants. J Food Sci 2003; 68: 487-90.
[http://dx.doi.org/10.1111/j.1365-2621.2003.tb05699.x]
[32]
Heo SJ, Park EJ, Lee KW, Jeon YJ. Antioxidant activities of enzymatic extracts from brown seaweeds. Bioresour Technol 2005; 96(14): 1613-23.
[http://dx.doi.org/10.1016/j.biortech.2004.07.013] [PMID: 15978995]
[33]
MacDonald-Wicks LK, Wood LG, Garg ML. Methodology for the determination of biological antioxidant capacity in vitro: A review. J Sci Food Agric 2006; 86(13): 2046-56.
[http://dx.doi.org/10.1002/jsfa.2603]
[34]
Aoshima H, Tsunoue H, Koda H, Kiso Y. Aging of whiskey increases 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity. J Agric Food Chem 2004; 52(16): 5240-4.
[http://dx.doi.org/10.1021/jf049817s] [PMID: 15291502]
[35]
Hyslop PA, Hinshaw DB, Halsey WA Jr. et al. Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J Biol Chem 1988; 263(4): 1665-75.
[http://dx.doi.org/10.1016/S0021-9258(19)77928-9] [PMID: 3338986]
[36]
Apak R, Özyürek M, Güçlü K, Çapanoğlu E. Antioxidant activity/capacity measurement: I. Classification, physicochemical principles, mechanisms and Electron Transfer (ET)-based assays. J Agric Food Chem 2016; 64(5): 997-1027.
[http://dx.doi.org/10.1021/acs.jafc.5b04739] [PMID: 26728425]
[37]
Zengin G, Guler G-O, Aktumsek A, Ceylan R, Picot CMN, Mahomoodally MF. Enzyme inhibitory properties, antioxidant activities, and phytochemical profile of three medicinal plants from Turkey. Adv Pharmacol Sci 2015; 2015: 410675.
[http://dx.doi.org/10.1155/2015/410675] [PMID: 26798334]
[38]
Zengin G, Locatelli M, Ceylan R, Aktumsek A. Anthraquinone profile, antioxidant and enzyme inhibitory effect of root extracts of eight Asphodeline taxa from Turkey: Can Asphodeline roots be considered as a new source of natural compounds? J Enzyme Inhib Med Chem 2016; 31(5): 754-9.
[http://dx.doi.org/10.3109/14756366.2015.1063623] [PMID: 26207512]
[39]
Wexler P. Encyclopedia of Toxicology. (3rd ed.), Academic press 2014.
[40]
Genç H, Kalin R, Köksal Z. et al. Discovery of potent carbonic anhydrase and acetylcholinesterase inhibitors: 2-aminoindan b-lactam derivatives. Int J Mol Sci 2016; 17(10): 1736.
[http://dx.doi.org/10.3390/ijms17101736] [PMID: 27775608]
[41]
Topal F, Gulcin I, Dastan A, Guney M. Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors. Int J Biol Macromol 2017; 94(Pt B): 845-51. http://dx.doi.org/10.1016/j.ijbiomac.2016.10.096 PMID: 27984137
[42]
Abirami A, Nagarani G, Siddhuraju P. In vitro antioxidant, anti-diabetic, cholinesterase and tyrosinase inhibitory potential of fresh juice from Citrus hystrix and C. maxima fruits. Food Sci Hum Wellness 2014; 3(1): 16-25.
[http://dx.doi.org/10.1016/j.fshw.2014.02.001]
[43]
Choi JS, Islam MN, Ali MY, Kim EJ, Kim YM, Jung HA. Effects of C-glycosylation on anti-diabetic, anti-Alzheimer’s disease and anti-inflammatory potential of apigenin. Food Chem Toxicol 2014; 64: 27-33.
[http://dx.doi.org/10.1016/j.fct.2013.11.020] [PMID: 24291393]
[44]
Senol FS, Orhan IE, Ustun O. In vitro cholinesterase inhibitory and antioxidant effect of selected coniferous tree species. Asian Pac J Trop Med 2015; 8(4): 269-75.
[http://dx.doi.org/10.1016/S1995-7645(14)60329-1] [PMID: 25975497]
[45]
World Health Organization (WHO). Dimentia. Available from: https://www.who.int/newsroom/factsheets/detail/dementia
[46]
Burns A, Iliffe S. Alzheimer’s disease. BMJ 2009; 338(feb05 1): b158.. http://dx.doi.org/10.1136/bmj.b158 PMID: 19196745
[47]
Peng X, Zhang G, Liao Y, Gong D. Inhibitory kinetics and mechanism of kaempferol on α-glucosidase. Food Chem 2016; 190: 207-15.
[http://dx.doi.org/10.1016/j.foodchem.2015.05.088] [PMID: 26212963]
[48]
Zaid H, Saad B, Mahdi AA, Tamrakar AK, Haddad PS, Afifi FU. Medicinal plants and natural active compounds for diabetes and/or obesi-ty treatment. Evid Based Complement Alternat Med 2015; 2015: 469762.
[http://dx.doi.org/10.1155/2015/469762] [PMID: 26557860]
[49]
Gurudeeban S, Satyavani K, Ramanathan T. Alpha glucosidase inhibitory effect and enzyme kinetics of coastal medicinal plants. Bangladesh J Pharmacol 2012; 7(3): 186-91.
[http://dx.doi.org/10.3329/bjp.v7i3.11499]
[50]
Zengin G, Sarikurkcu C, Aktumsek A, Ceylan R. Sideritis galatica Bornm.: A source of multifunctional agents for the management of oxi-dative damage, Alzheimer’s’s and diabetes mellitus. J Funct Foods 2014; 11: 538-47.
[http://dx.doi.org/10.1016/j.jff.2014.08.011]
[51]
Playford RJ, Pither C, Gao R, Middleton SJ. Use of the α glucosidase inhibitor acarbose in patients with ‘Middleton syndrome’: Normal gastric anatomy but with accelerated gastric emptying causing postprandial reactive hypoglycemia and diarrhea. Can J Gastroenterol 2013; 27(7): 403-4.
[http://dx.doi.org/10.1155/2013/791803] [PMID: 23862171]
[52]
Dressler H, Dawson CR. On the nature and mode of action of the copperprotein, tyrosinase. I. Exchange experiments with radioactive copper and the resting enzyme. Biochim Biophys Acta 1960; 45: 508-14.
[http://dx.doi.org/10.1016/0006-3002(60)91487-6] [PMID: 13724358]
[53]
Kim YJ, Uyama H. Tyrosinase inhibitors from natural and synthetic sources: Structure, inhibition mechanism and perspective for the future. Cell Mol Life Sci 2005; 62(15): 1707-23.
[http://dx.doi.org/10.1007/s00018-005-5054-y] [PMID: 15968468]
[54]
Du ZY, Jiang YF, Tang ZK. et al. Antioxidation and tyrosinase inhibition of polyphenolic curcumin analogs. Biosci Biotechnol Biochem 2011; 75(12): 2351-8.
[http://dx.doi.org/10.1271/bbb.110547] [PMID: 22146732]
[55]
Saewan N, Thakam A, Jintaisong A, Kittigoitana K. Anti-tyrosinase and cytotoxicity activities of curcumin-metal complexes. Int J Pharm Pharm Sci 2014; 6(10): 270-3.

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