Isaac Scientific Publishing

Journal of Advances in Molecular Biology

In Silico Comparison of Synthetic and Natural Molecules Bindings with Acetylcholinesterase Enzyme using Molecular Docking

Download PDF (1549.9 KB) PP. 17 - 26 Pub. Date: September 1, 2018

DOI: 10.22606/jamb.2018.23001

Author(s)

  • Fouzia Mesli
    Laboratory of Naturals Products and Bioactives- LASNABIO, University of Tlemcen. B. P. 119, 13000 Tlemcen. Algeria
  • Salim Bouchentouf*
    Laboratory of Naturals Products and Bioactives- LASNABIO, University of Tlemcen. B. P. 119, 13000 Tlemcen. Algeria;Faculty of Technology, Doctor Tahar Moulay University of Saida, Algeria
  • Amina Ghomri
    Laboratory of Naturals Products and Bioactives- LASNABIO, University of Tlemcen. B. P. 119, 13000 Tlemcen. Algeria;High school of Applied Sciences ESSA Tlemcen. B. P. 165, 13000 Tlemcen. Algeria
  • Noureddine Missoum
    Laboratory of Naturals Products and Bioactives- LASNABIO, University of Tlemcen. B. P. 119, 13000 Tlemcen. Algeria;Faculty of Scineces, Hassiba Benbouali University of Chlef, Algeria
  • Said Ghalem
    Laboratory of Naturals Products and Bioactives- LASNABIO, University of Tlemcen. B. P. 119, 13000 Tlemcen. Algeria

Abstract

Inhibition of Acetylcholinesterase (AChE) is an important approach for Alzheimer's disease (AD) treatment. Different synthetic and natural inhibitors are used for Acetylcholinesterase inhibition. Synthetic inhibitors Polyphenols (Tacrine, Donepezil, Rivastigmine, Galantamine) and Natural molecules from Green tea which mainly contains catechins (Epicatechin, Epicatechin Gallate, Epigallocatechin, Epigallocatechin Gallate) are used to inhibit Acetylcholinesterase. In this work we use molecular docking methods to identify the ligand which has the best interaction energy with AChE among synthetic and natural products, and also descript binding affinity in purpose to design new inhibitor ligands. Obtained results from Docking and analyze of complexes parameters showed that the best affinity binding was observed for both (Galantamie and Epicatechin Gallete).This latter leads to same conclusion with experimentation inhibition study. We observed also that bulky group causes conformational rearrangement in the active pocket, which will probably give better interactions.

Keywords

Alzheimer; acetylcholinesterase enzyme; polyphenol; green tea; molecular docking.

References

[1] Querfurth HW, LaFerla FM (2010) Alzheimer's disease. The New England Journal of Medicine 28 January 362 (4): 329–44.

[2] Todd S, Barr S, Roberts M, Passmore, AP (2013) Survival in dementia and predictors of mortality: a review. International Journal of Geriatric Psychiatry November 28 (11): 1109–24.

[3] Katergaris N, Dufficy L, Roach PD, Naumovski N (2015) Green tea catechins as neuroprotective agents: systematic review of the literature in animalpre-clinical trials. Adv Food Technol Nutr Sci Open J 1(2): 48-57.

[4] Lane, Roger M, Miia Kivipelto, and Nigel H (2004) Greig. Acetylcholinesterase and its inhibition in Alzheimer disease. Clinical neuropharmacology 27(3): 141-149.

[5] Khan MA, Hussain, A, Sundaram MK, et al. (2015) (-)-Epigallocatechin-3-gallate reverses the expression of various tumor-suppressor genes by inhibiting DNA methyltransferases and histone deacetylases in human cervical cancer cells. Oncol Rep 33(4): 1976-1984.

[6] Nabavi SM, Daglia M, Moghaddam AH, Nabavi SF, Curti V (2014) Tea consumption and risk of ischemic stroke: a brief review of the literature. Curr Pharm Biotechnol 15(4): 298-303.

[7] Matsushita K (2014) Epigallocatechin gallate suppresses LPS endocytosis and nitric oxide production by reducing Rab5-caveolin-1 interaction.Biomed Res. 35(2): 145-151.

[8] Cai J, Jing D, Shi M, et al. (2014) Epigallocatechin gallate (EGCG) attenuates infrasound-induced neuronal impairment by inhibiting microglia-mediated inflammation J Nutr Biochem 25(7): 716-725.

[9] Vuong QV, Golding JB, Nguyen M, Roach PD (2010) Extraction and isolation of catechins from tea. J Sep Sci 33(21): 3415-3428.

[10] Lee HS, Jun JH, Jung EH, Koo BA, Kim YS (2014)Epigalloccatechin-3-gallate inhibits ocular neovascularization and vascular permeability in human retinal pigment epithelial and human retinal microvascular endothelial cells via suppression of MMP-9 and VEGF activation. Molecules 19(8):12150-12172.

[11] Betts JW, Wareham DW (2014) In vitro activity of curcumin in combination with epigallocatechin gallate (EGCG) versus multidrug-resistant Acinetobacter baumannii. BMC Microbiol 14, 172

[12] Reygaert WC (2014) The antimicrobial possibilities of green tea. Front Microbiol 5, 434.

[13] Saiko P, Steinmann MT, Schuster H, et al. (2015) Epigallocatechin gallate, ellagic acid, and rosmarinic acid perturb dNTP pools and inhibit de novo DNA synthesis and proliferation of human HL-60 promyelocytic leukemia cells: Synergism with arabinofuranosylcytosine. Phytomedicine 22 (1): 213-222.

[14] Sussman JL, Harel M, Silman I. (1993) Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs. Chem. Biol. Interact. June 87 (1–3): 187–97.

[15] Colovic MB, Krstic, Danijela Z, Lazarevic-Pasti, Tamara D, Bondzic, Aleksandra M, Vasic, Vesna M (2013) Acetylcholinesterase Inhibitors: Pharmacology and Toxicology. Current Neuropharmacology 11 (3): 315–335.

[16] Bezerra da Silva, Cristiane, et al. (2016) Effect of donepezil, tacrine, galantamine and rivastigmine on acetylcholinesterase inhibition in Dugesia tigrina. Molecules 21.1: 53.

[17] Sugimoto H, Iimura Y, Yamanishi Y, Yamatsu K (1992) Synthesis and anti-acetylcholinesterase activity of 1-benzyl-4-[5, 6-dimethoxy-1-indanon-2-yl] methylpiperidine hydrochloride (E2020) and related compounds. Bioorg Med Chem Lett 2: 871–876

[18] Anand R, Gharabawi G, Enz A (1996) Efficacy and safety results of the early phase studies with Exelon (ENA 713) in Alzheimer's disease: an overview. J Drug Dev Clin Pract 8: 109–116.

[19] Heinrich M, Teoh HL (1992) Galanthamine from snowdrop – the development of a modern drug against Alzheimer's disease from local Caucasian knowledge. Journal of Ethnopharmacology (2–3): 147–162.

[20] Selen A, Balogh L, Siedlik P (1988) Pharmacokinetics of tacrine in healthy subjects. Pharm Res. 5: 218.

[21] Raja S (2017) INVESTIGATION OF HEPATOPROTECTIVE AND ANTIOXIDANT ACTIVITIES OF INDIAN MEDICINAL PLANTS.

[22] Molecular Operating Environment (MOE), Chemical Computing Group, Montreal, Quebec, Canada10, 2013.

[23] Powers JP, Piper DE, Li Y, Mayorga V, Anzola J, Chen JM, et al. (2006) SAR and mode of action of novel non-nucleoside inhibitors of hepatitis C NS5b RNA polymerase. J Med Chem 49(3).

[24] Goto J, Kataoka R, Muta H, and al. (2008) ASEDock-docking based on alpha spheres and excluded volumes J Chem Inf Model 48, 583-590.

[25] Manikrao AM, Mahajan1 NS, Jawarkar RD, Mahajan DT, Masand2 VH, TBen Hadda (2011) Docking Studies of few C-3 Substituted Azapteridines as Hepatitis C Virus RNA-Dependent RNA Polymerase inhibitors Scholars Research Library. J. Comput. Method. Mol. Design 35-45.

[26] Labute P, Williams C, Feher M, Sourial E, Schmidt JM. (2001) Flexible alignment of small molecules J. Med. Chem. 44:1483-1490.

[27] (a) Clark AM, Labute P, Santavy M (2006) Journal of chemical information and modeling . J. Chem.46, Inf. Model. 1107-1123.

[28] Clark AM, Labute P (2008) Clark, A. M., & Labute, P. (2008). Detection and assignment of common scaffolds in project databases of lead molecules J. Med. Chem. 52: 469-483

[29] Ritchie D, Macromolecular Docking Using Spherical Polar Fourier Correlations, Department of Computing Science, University of Aberdeen, copyright ? 1996-2005

[30] Yamaguchi H, Kamiie K, Kidachi Y, Noshita T, Umetsu H, Fuke, Y, Ryoyama K (2014). Intracellular accumulation of structurally varied isothiocyanates correlates with inhibition of nitric oxide production in proinflammatory stimuli-activated tumorigenic macrophage-like cells. Bioorganic & medicinal chemistry 22(1): 440-446.

[31] Lipinski CA. (2004). Lead- and drug-like compounds: The rule-of-five revolution. Drug Discovery Today: Technologies.1 (4):337-342.

[32] Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. (1997). Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev.23:3–25.