Research Article
BibTex RIS Cite

Year 2022, , 66 - 71, 30.03.2022

Yasemin Camadan , Ebru Akkemik

https://doi.org/10.17776/csj.983869
Cited By: 3

Abstract

Supporting Institution

Artvin Çoruh Üniversitesi

Project Number

BAP. 2016.M80.02.09

References

  • [1] Mantoani S.P., Chierrito P.C.T., Vilela F.L.A., Cardoso L.C., Martínez A., Carvalho I., Novel Triazole-Quinoline Derivatives as Selective Dual Binding Site Acetylcholinesterase Inhibitors, Molecules, 193(21) (2016).
  • [2] Prasasty V., Radifar M., Istyastono E., Natural Peptides in Drug Discovery Targeting Acetylcholinesterase, Molecules, 2344(21) (2018).
  • [3] Liu P.P., Xie Y., Meng Y.X., Kang S.J., History And Progress Of Hypotheses And Clinical Trials For Alzheimer’s Disease, Signal Transduct Target Ther, 4 (29) (2019).
  • [4] Vicente-Zurdo D., Romero-Sánchez I., Rosales-Conrado N., León-González M.E., Madrid Y., Ability Of Selenium Species To Inhibit Metal-Induced Aβ Aggregation Involved In The Development Of Alzheimer’s Disease, Anal. Bioanal. Chem., 412 (2020) 6485-6497.
  • [5] Askar A.K., Kudi C.A., Moody J.A., Purification of Soluble Acetylcholinesterase from Sheep Liver by Affinity Chromatography, Appl Biochem Biotechnol., 165 (2011) 336–346.
  • [6] Zhang Y., Hei T., Cai Y., Gao Q., Zhang Q., Affinity Binding-Guided Fluorescent Nanobiosensor for Acetylcholinesterase Inhibitors via Distance Modulation between the Fluorophore and Metallic Nanoparticle, Anal. Chem., 84 (2012) 2830−2836.
  • [7] He T., Qi L., Zhang J., Huang L.Y., Zhang Q.Z., Enhanced Graphene Quantum Dot Fluorescence Nanosensor For Highly Sensitive Acetylcholinesterase Assay And Inhibitor Screening, Sensors and Actuators B, 215 (2015) 24–29.
  • [8] Zhu L.H., Liu W.Y., Liu W.W., Yin J.F., Caoa L.Z., Baoa J., Lia M., Qina Y.L., Shia H.D., Synthesis, Characterisation And Acetylcholinesterase-Inhibition Activities Of 5-Benzyl-1,3,4-Thiadiazol-2-Amine Derivatives, J. Chem. Phys., 40 (2016).
  • [9] Akbulut G., Akkemik E., Investigation of Inhibition Effects Of Honey, Pollen, Propolis And Royal Jelly Extracts On Thioredoxinreductase Enzyme Activity, SAUJS, 22(6) (2018) 1585-1590.
  • [10] Youdim A. K., Joseph A.J., A Possible Emerging Role Of Phytochemicals In Improving Age-Related Neurological Dysfunctions: A Multiplicity Of Effects, Free Radical Biology & Medicine, 30(6) (2001) 583–594.
  • [11] Gomez-Caracava A.M., Gomez-Romero M., Arraez-Roman D., Segura-Carretero A., Fernandez-Gutierrez A., Advances In The Analysis Of Phenolic Compounds In Products Derived From Bees, J. Pharm. Biomed. Anal., 41 (2006) 1220–1234.
  • [12] Sahin H., Aliyazicioglu R., Yildiz O., Kolayli A., Innocenti A., Supuran T.C., Honey, Polen, And Propolis Extracts Show Potent Inhibitory Activity Against The Zinc Metalloenzyme Carbonic Anhydrase, J. Enzyme Inhib. Med. Chem., 26(3) (2011) 440–444.
  • [13] Olas B., Honey and Its Phenolic Compounds as an Effective Natural Medicine for Cardiovascular Diseases in Humans?, Nutrients, 283 (12) (2020).
  • [14] Kösoğlu M., Yücel B., Gökbulut C., Konak R., Bircan C., The Effect of Harvesting Time on Some Biochemical and Trace Element Compositions of Royal Jelly, Kafkas Univ. Vet. Fak. Derg., 19(2) (2013) 233-237.
  • [15] Crozier A., Jaganath B.I., Clifford N.M., Dietary Phenolics: Chemistry, Bioavailability And Effects On Health, Nat. Prod. Rep., 26 (2009) 1001-1043.
  • [16] Chen G-L., Chen S-G., Chen F., Xie Y-Q., Han M-D., Luo C-X., Zhao Y-Y., Gao Y-Q., Nutraceutical Potential And Antioxidant Benefits Of Selected Fruit Seeds Subjected To An In Vitro Digestion, J. Funct. Foods, 20 (2016) 317–331.
  • [17] Alyes E., Simoes A., Domingues R., Fruit Seeds And Their Oils As Promising Sources Of Value-Added Lipids From Agro-İndustrial By Products: Oil Content, Lipid Composition, Lipid Analysis, Biological Activity And Potential Biotechnological Applications, Crit. Rev. Food Sci. Nutr.,61(8) (2021) 1305–1339.
  • [18] Gasparotto J., Somensi N., Bortolin C.R., Moresco S.K., Girardi S.C., Klafke K., Rabelo K.T., Morrone S.M., Vizzotto M., Raseira B.C.M., Moreira F.C.J., Gelain P.D., Effects Of Different Products Of Peach (Prunuspersica L. Batsch) From A Variety Developed In Southern Brazil On Oxidative Stress And Inflammatory Parameters In Vitro And Ex Vivo, J. Clin. Biochem.Nutr., 55(2) (2014) 110–119.
  • [19] Rai I., Bachheti K.R., Saini K.C., Joshi A., Satyan S.R., A Review On Phytochemical, Biological Screening And Importance of Wild Apricot (Prunusarmeniaca L.), Orient Pharm. Exp. Med., (2015).
  • [20] Ozturk B., Kucukera E., Karaman S., Ozkana Y., The Effects Of Cold Storage And Aminoethoxyvinylglycine (AVG) On Bioactive Compounds Of Plum Fruit (PrunussalicinaLindell cv. ‘Black Amber’), Postharvest Biol. Technol., 72 (2012) 35–41.
  • [21] Yoo M.K., Al-Farsi M., Lee H., Yoon H., Lee Y.C., Antiproliferative Effects Of Cherry Juice And Wine In Chinese Hamster Lung Fibroblast Cells And Their Phenolic Constituents And Antioxidant Activities, Food Chem., 123 (2010) 734–740.
  • [22] Velioğlu S., Determination Of Antioxidant And Antibacterial Activities And Phenolic Compounds Distribution Of Different Tea Extracts by HPLC, Ankara University Scientific Research Projects, Ankara University, 2007.
  • [23] Ellman G.L., Courtney D.K., Andres V., Featherstone M.R., New and Rapid Colorimetric Determination Of Acetylcholinesterase Activity, Biochem. Pharmacol, 7 (1961) 88-95.
  • [24] Caglayan C., Taslimi P., Türk C., Kandemir M.F., Demir Y., Gulcin İ., Purification And Characterization Of The Carbonic Anhydrase Enzyme From Horse Mackerel (Trachurustrachurus) Muscle And The Impact Of Some Metal Ions And Pesticides On Enzyme Activity, Comp. Biochem. Physiol , 226 (2019) 108605.
  • [25] Lineweaver H., Burk, D., The Determination Of Enzyme Dissociation Constants, J. Am. Chem. Soc., 56 (1934) 658–666.
  • [26] Zhang X., Feng P., Gao X., Wang B., Gou C., Bian R., In Vitro Inhibitory Effects Of Cepharanthine On Human Liver Cytochrome P450 Enzymes, Pharm. Biol., 58(1) (2020) 247–252.
  • [27] Silva I.J., Moraes C.M., Vieira C.C.L., Corrêa G.A., Cass B.Q, Cardoso L.C., Acetylcholinesterase Capillary Enzyme Reactor For Screening And Characterization Of Selective Inhibitors, J. Pharm. Biomed., 73 (2013) 44– 52.
  • [28] Yildiz O., Karahalil F., Can Z., Sahin H., Kolayli S., Total Monoamine Oxidase (MAO) Inhibition By Chestnut Honey, Pollen And Propolis, J. Enzyme Inhib. Med. Chem., 29(5) (2014) 690–694.
  • [29] Kolayli S., Can Z., Yildiz O., Sahin H., Karaoglu A. S., A Comparative Study Of The Antihyaluronidase, Antiurease, Antioxidant, Antimicrobial And Physicochemical Properties Of Different Unifloral Degrees Of Chestnut (Castanea sativa Mill.) Honeys, J. Enzyme Inhib. Med. Chem
  • [30] Tkacz K., Wojdyło A., Nowicka P., Turkiewicz I., Golis T., Characterization In Vitro Potency Of Biological Active Fractions Of Seeds, Skins And Flesh From Selected Vitisvinifera L. Cultivars And Interspecific Hybrids, J. Funct. Foods, 56 (2019). 353–63.
  • [31] Lakshmi Thangavelu T., Ramasamy R., In vitro Acetyl Cholinesterase Inhibitory assay of Acacia catechu Willd Ethanolic Seed Extract, Pharmacognosy J., 7(5) (2015).
  • [32] Oboh G., J. Akinyemi J.A., Omojokun S.O., Oyeleye S.I., Anticholinesterase and Antioxidative Properties of Aqueous Extract of Cola acuminata Seed In Vitro, Int. J. Alzheimers Dis., (2014) 1-8.
  • [33] Kumar S., Chowdhury S., Kinetics Of Acetylcholinesterase Inhibition By An Aqueous Extract Of Cuminum Cyminum Seeds, Int. J. Appl. Sci. Biotechnol., 2(1) (2014) 64-68.
  • [34] Chaibi R., Drine S., Ferchichi A., Chemical Study And Biological Activities Of Various Extracts From Lawsonia Inermis (Henna) Seeds, Acta Medica Mediterr, 33 (2017) 981-986.

Searching for New Natural Inhibitors of Acetylcholinesterase Enzyme

Year 2022, , 66 - 71, 30.03.2022

Yasemin Camadan , Ebru Akkemik

https://doi.org/10.17776/csj.983869
Cited By: 3

Abstract

Acetylcholinesterase enzyme (AChE) is the enzyme that catalyzes the hydrolysis of the neurotransmitter acetylcholine to choline. Inhibitors of this enzyme (AChE-i) are used to treat Alzheimer's, a neurodegenerative disease. Due to the side effects of the drugs used, there has been an increased interest in investigating the inhibitory potentials of natural products which are presumed to have fewer side effects. For this purpose, the inhibitory effects of highland honey, chestnut honey, royal jelly and the seeds of peach, cherry, plum and apricot on human erythrocyte AChE enzyme was investigated in vitro in the present study. Extracts of the seeds and bee products were prepared in ethanol solvent. In order to determine the inhibitory effect of the extracts, the inhibition concentration (IC50) and Ki values which cause 50% inhibition of the enzyme were calculated using the Ellman method. It was found that among the natural product extracts studied, peach seed had the highest inhibition level (IC50 value 0.05708 mg/ml). IC50 values of highland honey, royal jelly, plum seed and apricot seed were determined as 0.2555 (mg/mL), 0.300 (mg/mL), 0.7049 (mg/mL) and 0.4544 (mg/mL) respectively.

Keywords

Alzheimer’ AChE Inhibition Bee products Fruit seeds

Project Number

BAP. 2016.M80.02.09

References

  • [1] Mantoani S.P., Chierrito P.C.T., Vilela F.L.A., Cardoso L.C., Martínez A., Carvalho I., Novel Triazole-Quinoline Derivatives as Selective Dual Binding Site Acetylcholinesterase Inhibitors, Molecules, 193(21) (2016).
  • [2] Prasasty V., Radifar M., Istyastono E., Natural Peptides in Drug Discovery Targeting Acetylcholinesterase, Molecules, 2344(21) (2018).
  • [3] Liu P.P., Xie Y., Meng Y.X., Kang S.J., History And Progress Of Hypotheses And Clinical Trials For Alzheimer’s Disease, Signal Transduct Target Ther, 4 (29) (2019).
  • [4] Vicente-Zurdo D., Romero-Sánchez I., Rosales-Conrado N., León-González M.E., Madrid Y., Ability Of Selenium Species To Inhibit Metal-Induced Aβ Aggregation Involved In The Development Of Alzheimer’s Disease, Anal. Bioanal. Chem., 412 (2020) 6485-6497.
  • [5] Askar A.K., Kudi C.A., Moody J.A., Purification of Soluble Acetylcholinesterase from Sheep Liver by Affinity Chromatography, Appl Biochem Biotechnol., 165 (2011) 336–346.
  • [6] Zhang Y., Hei T., Cai Y., Gao Q., Zhang Q., Affinity Binding-Guided Fluorescent Nanobiosensor for Acetylcholinesterase Inhibitors via Distance Modulation between the Fluorophore and Metallic Nanoparticle, Anal. Chem., 84 (2012) 2830−2836.
  • [7] He T., Qi L., Zhang J., Huang L.Y., Zhang Q.Z., Enhanced Graphene Quantum Dot Fluorescence Nanosensor For Highly Sensitive Acetylcholinesterase Assay And Inhibitor Screening, Sensors and Actuators B, 215 (2015) 24–29.
  • [8] Zhu L.H., Liu W.Y., Liu W.W., Yin J.F., Caoa L.Z., Baoa J., Lia M., Qina Y.L., Shia H.D., Synthesis, Characterisation And Acetylcholinesterase-Inhibition Activities Of 5-Benzyl-1,3,4-Thiadiazol-2-Amine Derivatives, J. Chem. Phys., 40 (2016).
  • [9] Akbulut G., Akkemik E., Investigation of Inhibition Effects Of Honey, Pollen, Propolis And Royal Jelly Extracts On Thioredoxinreductase Enzyme Activity, SAUJS, 22(6) (2018) 1585-1590.
  • [10] Youdim A. K., Joseph A.J., A Possible Emerging Role Of Phytochemicals In Improving Age-Related Neurological Dysfunctions: A Multiplicity Of Effects, Free Radical Biology & Medicine, 30(6) (2001) 583–594.
  • [11] Gomez-Caracava A.M., Gomez-Romero M., Arraez-Roman D., Segura-Carretero A., Fernandez-Gutierrez A., Advances In The Analysis Of Phenolic Compounds In Products Derived From Bees, J. Pharm. Biomed. Anal., 41 (2006) 1220–1234.
  • [12] Sahin H., Aliyazicioglu R., Yildiz O., Kolayli A., Innocenti A., Supuran T.C., Honey, Polen, And Propolis Extracts Show Potent Inhibitory Activity Against The Zinc Metalloenzyme Carbonic Anhydrase, J. Enzyme Inhib. Med. Chem., 26(3) (2011) 440–444.
  • [13] Olas B., Honey and Its Phenolic Compounds as an Effective Natural Medicine for Cardiovascular Diseases in Humans?, Nutrients, 283 (12) (2020).
  • [14] Kösoğlu M., Yücel B., Gökbulut C., Konak R., Bircan C., The Effect of Harvesting Time on Some Biochemical and Trace Element Compositions of Royal Jelly, Kafkas Univ. Vet. Fak. Derg., 19(2) (2013) 233-237.
  • [15] Crozier A., Jaganath B.I., Clifford N.M., Dietary Phenolics: Chemistry, Bioavailability And Effects On Health, Nat. Prod. Rep., 26 (2009) 1001-1043.
  • [16] Chen G-L., Chen S-G., Chen F., Xie Y-Q., Han M-D., Luo C-X., Zhao Y-Y., Gao Y-Q., Nutraceutical Potential And Antioxidant Benefits Of Selected Fruit Seeds Subjected To An In Vitro Digestion, J. Funct. Foods, 20 (2016) 317–331.
  • [17] Alyes E., Simoes A., Domingues R., Fruit Seeds And Their Oils As Promising Sources Of Value-Added Lipids From Agro-İndustrial By Products: Oil Content, Lipid Composition, Lipid Analysis, Biological Activity And Potential Biotechnological Applications, Crit. Rev. Food Sci. Nutr.,61(8) (2021) 1305–1339.
  • [18] Gasparotto J., Somensi N., Bortolin C.R., Moresco S.K., Girardi S.C., Klafke K., Rabelo K.T., Morrone S.M., Vizzotto M., Raseira B.C.M., Moreira F.C.J., Gelain P.D., Effects Of Different Products Of Peach (Prunuspersica L. Batsch) From A Variety Developed In Southern Brazil On Oxidative Stress And Inflammatory Parameters In Vitro And Ex Vivo, J. Clin. Biochem.Nutr., 55(2) (2014) 110–119.
  • [19] Rai I., Bachheti K.R., Saini K.C., Joshi A., Satyan S.R., A Review On Phytochemical, Biological Screening And Importance of Wild Apricot (Prunusarmeniaca L.), Orient Pharm. Exp. Med., (2015).
  • [20] Ozturk B., Kucukera E., Karaman S., Ozkana Y., The Effects Of Cold Storage And Aminoethoxyvinylglycine (AVG) On Bioactive Compounds Of Plum Fruit (PrunussalicinaLindell cv. ‘Black Amber’), Postharvest Biol. Technol., 72 (2012) 35–41.
  • [21] Yoo M.K., Al-Farsi M., Lee H., Yoon H., Lee Y.C., Antiproliferative Effects Of Cherry Juice And Wine In Chinese Hamster Lung Fibroblast Cells And Their Phenolic Constituents And Antioxidant Activities, Food Chem., 123 (2010) 734–740.
  • [22] Velioğlu S., Determination Of Antioxidant And Antibacterial Activities And Phenolic Compounds Distribution Of Different Tea Extracts by HPLC, Ankara University Scientific Research Projects, Ankara University, 2007.
  • [23] Ellman G.L., Courtney D.K., Andres V., Featherstone M.R., New and Rapid Colorimetric Determination Of Acetylcholinesterase Activity, Biochem. Pharmacol, 7 (1961) 88-95.
  • [24] Caglayan C., Taslimi P., Türk C., Kandemir M.F., Demir Y., Gulcin İ., Purification And Characterization Of The Carbonic Anhydrase Enzyme From Horse Mackerel (Trachurustrachurus) Muscle And The Impact Of Some Metal Ions And Pesticides On Enzyme Activity, Comp. Biochem. Physiol , 226 (2019) 108605.
  • [25] Lineweaver H., Burk, D., The Determination Of Enzyme Dissociation Constants, J. Am. Chem. Soc., 56 (1934) 658–666.
  • [26] Zhang X., Feng P., Gao X., Wang B., Gou C., Bian R., In Vitro Inhibitory Effects Of Cepharanthine On Human Liver Cytochrome P450 Enzymes, Pharm. Biol., 58(1) (2020) 247–252.
  • [27] Silva I.J., Moraes C.M., Vieira C.C.L., Corrêa G.A., Cass B.Q, Cardoso L.C., Acetylcholinesterase Capillary Enzyme Reactor For Screening And Characterization Of Selective Inhibitors, J. Pharm. Biomed., 73 (2013) 44– 52.
  • [28] Yildiz O., Karahalil F., Can Z., Sahin H., Kolayli S., Total Monoamine Oxidase (MAO) Inhibition By Chestnut Honey, Pollen And Propolis, J. Enzyme Inhib. Med. Chem., 29(5) (2014) 690–694.
  • [29] Kolayli S., Can Z., Yildiz O., Sahin H., Karaoglu A. S., A Comparative Study Of The Antihyaluronidase, Antiurease, Antioxidant, Antimicrobial And Physicochemical Properties Of Different Unifloral Degrees Of Chestnut (Castanea sativa Mill.) Honeys, J. Enzyme Inhib. Med. Chem
  • [30] Tkacz K., Wojdyło A., Nowicka P., Turkiewicz I., Golis T., Characterization In Vitro Potency Of Biological Active Fractions Of Seeds, Skins And Flesh From Selected Vitisvinifera L. Cultivars And Interspecific Hybrids, J. Funct. Foods, 56 (2019). 353–63.
  • [31] Lakshmi Thangavelu T., Ramasamy R., In vitro Acetyl Cholinesterase Inhibitory assay of Acacia catechu Willd Ethanolic Seed Extract, Pharmacognosy J., 7(5) (2015).
  • [32] Oboh G., J. Akinyemi J.A., Omojokun S.O., Oyeleye S.I., Anticholinesterase and Antioxidative Properties of Aqueous Extract of Cola acuminata Seed In Vitro, Int. J. Alzheimers Dis., (2014) 1-8.
  • [33] Kumar S., Chowdhury S., Kinetics Of Acetylcholinesterase Inhibition By An Aqueous Extract Of Cuminum Cyminum Seeds, Int. J. Appl. Sci. Biotechnol., 2(1) (2014) 64-68.
  • [34] Chaibi R., Drine S., Ferchichi A., Chemical Study And Biological Activities Of Various Extracts From Lawsonia Inermis (Henna) Seeds, Acta Medica Mediterr, 33 (2017) 981-986.
There are 34 citations in total.

Details

Primary Language English
Journal Section Natural Sciences
Authors

Yasemin Camadan 0000-0002-9000-7761

Ebru Akkemik 0000-0002-4177-4884

Project Number BAP. 2016.M80.02.09
Publication Date March 30, 2022
Submission Date August 17, 2021
Acceptance Date March 4, 2022
Published in Issue Year 2022

Cite

APA Camadan, Y., & Akkemik, E. (2022). Searching for New Natural Inhibitors of Acetylcholinesterase Enzyme. Cumhuriyet Science Journal, 43(1), 66-71. https://doi.org/10.17776/csj.983869

Cited By

Unveiling the Potential of Apricot Residues: From Nutraceuticals to Bioenergy
Waste
https://doi.org/10.3390/waste2010001
Tyrosinase Inhibitory Peptides from Enzyme Hydrolyzed Royal Jelly: Production, Separation, Identification and Docking Analysis
Foods
https://doi.org/10.3390/foods12112240
The potential of apricot seed and oil as functional food: Composition, biological properties, health benefits & safety
Food Bioscience
https://doi.org/10.1016/j.fbio.2022.102336