α-Cyperone of Cyperus rotundus is an effective candidate for reduction of inflammation by destabilization of microtubule fibers in brain

Journal of Ethnopharmacology

Volumn 194, Issue , 2016, Pages 219-227

  Azimi, Azam ^a   Ghaffari, Seyed Mahmood ^a   Riazi, Gholam Hossein ^a   Arab, Seyed Shahriar ^b   Tavakol, Mohammad Mehdi ^c   Pooyan, Shahriar ^a  

^a UNIVERSITY OF TEHRAN   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

^c ALLAMEH TABATABA'I UNIVERSITY   (Iran)

Author keywords

Microtubule polymerization; Molecular docking; Rhizomes of Cyperus rotundus; Tubulin; Cyperone

Indexed keywords

ALPHA CYPERONE; AMINO ACID; ANTIINFLAMMATORY AGENT; BETA TUBULIN; MICROTUBULE PROTEIN; TERPENOID; TUBULIN; UNCLASSIFIED DRUG; ALPHA-CYPERONE; NAPHTHALENE DERIVATIVE;

ANTIINFLAMMATORY ACTIVITY; ARTICLE; BINDING AFFINITY; BINDING SITE; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CYPERUS ROTUNDUS; DRUG PROTEIN BINDING; FLUORESCENCE SPECTROSCOPY; IN VITRO STUDY; LIGAND BINDING; MICROTUBULE ASSEMBLY; MOLECULAR DOCKING; MOLECULAR INTERACTION; NONHUMAN; POLYMERIZATION; PROTEIN SECONDARY STRUCTURE; RHIZOME; TRANSMISSION ELECTRON MICROSCOPY; TURBIDIMETRY; ANIMAL; BRAIN; CHEMISTRY; CYPERUS; DRUG EFFECTS; INFLAMMATION; MICROTUBULE; POLYACRYLAMIDE GEL ELECTROPHORESIS; SHEEP; SPECTROFLUOROMETRY;

ANIMALS; BRAIN; CIRCULAR DICHROISM; CYPERUS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; INFLAMMATION; MICROSCOPY, ELECTRON, TRANSMISSION; MICROTUBULES; MOLECULAR DOCKING SIMULATION; NAPHTHALENES; SHEEP; SPECTROMETRY, FLUORESCENCE;

EID: 84987861911     PISSN: 03788741     EISSN: 18727573     Source Type: Journal    
DOI: 10.1016/j.jep.2016.06.058     Document Type: Article

References (40)

1. Amos, L.A., Löwe, J., How Taxol stabilises microtubule structure. Chem. Biol. 6:3 (1999), 65–69.
2. Ben-Chetrit, E., Bergmann, S., Sood, R., Mechanism of the anti-inflammatory effect of colchicine in Rheumatic Diseases: a possible new outlook through microarray analysis. Rheumatology 45:3 (2006), 274–282.
3. Chakraborti, S., Das, L., Kapoor, N., Dasj, A., Dwivedi, V., Poddar, A., Chakraborti, G., Janik, M., Basu, G., Panda, D., Chakraborti, P., Surolia, A., Bhattacharyya, B., Curcumin recognizes a unique binding site of tubulin. J. Med. Chem. 54 (2011), 6183–6196.
4. Dadras, A., Riazi, G.H., Afrasiabi, A., Naghshineh, A., Ghalandari, B., Mokhtari, F., In vitro study on the alterations of brain tubulin structure and assembly affected by magnetite nanoparticles. J. Biol. Inorg. Chem. 18:3 (2013), 357–369.
5. 2+ in acidic aqueous media. J. Lumin. 132:8 (2012), 1987–1993.
6. Divsalar, A., Saboury, A.A., Binding Properties of a New Anti-tumor Component (2, 2′ -bipyridin octylglycinato Pd (II) nitrate) with Bovine β -lactoglobulin-A and -B. J. Biomol. Struct. Dyn. 25:2 (2014), 173–182.
7. Downing, K.H., Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 16 (2000), 89–111.
8. Durrant, J.D., Mccammon, J.A., BINANA : a novel algorithm for ligand-binding characterization. J. Mol. Graph. Model. 29:6 (2011), 888–893.
9. Faber, J., Pinguelli, L., Information processing in brain microtubules. BioSystems 83 (2006), 1–9.
10. Gaskin, F., Cantor, C.R., Shelanski, M.L., Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J. Mol. Biol. 89 (1974), 737–758.
11. Goodsell, D.S., Morris, G.M., Olson, A.J., Automated docking of flexible ligands : applications of AutoDock. J. Mol. Recognit. 9 (1996), 1–5.
12. Hamel, E., Antimitotic natural products and their interactions with tubulin. Med. Res. Rev. 16:2 (1996), 207–231.
13. Hameroff, S.R., Information processing in microtubules. J. Theor. Biol. 98 (1982), 549–561.
14. Hemmateenejad, B., Yousefinejad, S., Interaction study of human serum albumin and ZnS nanoparticles using fluorescence spectrometry. J. Mol. Struct. 1037 (2013), 317–322.
15. Irwin, J.J., Shoichet, B.K., ZINC – a free database of commercially available compounds for virtual screening. J. Chem. Inf. Model. 45:1 (2005), 177–182.
16. Jackman, R.W., Rhoads, M.G., Cornwell, E., Kandarian, S.C., Microtubule-mediated NF-κB activation in the TNF- α signaling pathway. Exp. Cell Res. 315:19 (2009), 3242–3249.
17. Jayabharathi, J., Thanikachalam, V., Srinivasan, N., Perumal, M.V., Luminescent study on the binding interaction of bioactive imidazole with bovine serum albumin-a static quenching mechanism. Spectrochim. Acta Part A: Mol. Biomol. Spectrosc. 84 (2011), 233–237.
18. Jebasingh, D., Jackson, D.D., Venkataraman, S., Emerald, B.S., Physiochemical and toxicological studies of the medicinal plant Cyperus rotundus L. (Cyperaceae). Int. J. Appl. Res. Nat. Prod. 5:4 (2013), 1–8.
19. Jung, S., Kim, S.J., Jung, S., Jun, B., Lee, K., Hong, S., Oh, M.S., Jang, D.S., Choi, J., α-Cyperone, isolated from the rhizomes of Cyperus rotundus, inhibits LPS-induced COX-2 expression and PGE2 production through the negative regulation of NF-κB signalling in RAW 264.7 cells. J. Ethnopharmacol. 147:1 (2013), 208–214.
20. Karin, M., Ben-neriah, Y., Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18 (2000), 621–663.
21. Keates, R.A.B., Microtubule associated proteins in microtubule preparations made with and without glycerol. Can. J. Biochem. Cell Biol. 62:9 (1984), 803–813.
22. Laskowski, R.A., Swindells, M.B., LigPlot +: Multiple ligand - protein interaction diagrams for drug discovery. J. Chem. Inf. Model. 51 (2011), 2778–2786.
23. Lim, G.P., Yang, F., Chu, T., Chen, P., Beech, W., Teter, B., Tran, T., Ubeda, O., Hasiao, A., Frautschy, S.A., Cole, G.M., Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer's disease. J. Neurosci. 20:15 (2000), 5709–5714.
24. Miller, H.P., Wilson, L., 2010. Isolation and biochemistry of tubulin and characterization of antibodies and isotypes, preparation of microtubule protein and purified tubulin from bovine brain by cycles of assembly and disassembly and phosphocellulose chromatography. Methods in Cell Biology: Volume 95 (First edit) Elsevier, pp. 2–15.
25. Minoura, I., Muto, E., Dielectric measurement of individual microtubules using the electroorientation method. Biophys. J. 90:10 (2006), 3739–3748.
26. Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., Olson, A.J., Automated docking using a Lamarckian Genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19:14 (1998), 1639–1662.
27. Morris, G.M., Huey, R., Lindstrom, W., Sanner, M.F., Belew, R.K., Goodsell, D.S., Olson, A.J., Software news and updates AutoDock4 and AutoDockTools4 : automated docking with selective receptor flexibility. J. Comput. Chem. 30:16 (2009), 2785–2791.
28. Nogales, E., Downing, K.H., Amos, L.A., Lӧwe, J., Tubulin and FtsZ form a distinct family of GTPases. Nat. Struct. Biol. 5:6 (1998), 451–458.
29. Rabiei, Z., Hojjati, M., Rafieian-kopaeia, M., Alibabaei, Z., Effect of Cyperus rotundus tubers ethanolic extract on learning and memory in animal model of Alzheimer, Biomedicine & Aging. Pathology 3 (2013), 185–191.
30. Ravelli, B.G.R., Gigant, B., Curmi, P.A., Jourdain, I., Lachkar, S., Sobel, A., Knossow, M., Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428 (2004), 198–202.
31. Redd, M.J., Kelly, G., Dunn, G., Way, M., Martin, P., Imaging macrophage chemotaxis in vivo: Studies of microtubule function in zebrafish wound inflammation. Cell Motil. Cytoskelet. 63:7 (2006), 415–422.
32. Seo, W., Pae, H., Oh, G., Chai, K., Kwon, T., Yun, Y., Kim, N., Chung, H., Inhibitory effects of methanol extract of Cyperus rotundus rhizomes on nitric oxide and superoxide productions by murine macrophage cell line, RAW 264.7 cells. J. Ethnopharmacol. 76 (2001), 59–64.
33. Soman, V.C., Sahane, R., Wankhade, V.M., Nandi, P., Karmarkar, C.S., Gokhale, M.R., Effect of Cyperus rotundus Root extract in midazolam induced memory loss in mice. Int. J. Pharmacol. Sci. Revolut. Res. 22:1 (2013), 269–272.
34. Sunil, A.G., Kesavanarayanan, K.S., Kalaivani, P., Sathiya, S., Ranju, V., Priya, R.J., Pramila, B., Paul, F.D.S., Venkhatesh, J., Babu, C.S., Total oligomeric flavonoids of Cyperus rotundus ameliorates neurological deficits, excitotoxicity and behavioral alterations induced by cerebral ischemic – reperfusion injury in rats. Brain Res. Bull. 84 (2011), 394–405.
35. Tabassum, S., Al-asbahy, W.M., Afzal, M., Arjmand, F., Synthesis, characterization and interaction studies of copper based drug with human serum albumin (HSA): spectroscopic and molecular docking investigations. J. Photochem. Photobiol. B : Biol. 114 (2012), 132–139.
36. Wallace, A.C., Laskowski, R.A., Thornton, J.M., Ligplot : a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:2 (1995), 127–134.
37. Wang, G., Peng, Q., Li, Y., Lanthanide-doped nanocrystals: synthesis, optical-magnetic properties, and applications. Acc. Chem. Res. 44:5 (2011), 322–332.
38. Wyss-Coray, T., Rogers, J., 2012. Inflammation in Alzheimer disease-A brief review of the basic science and clinical literature. Cold Spring Harbor Perspectives in Medicine, 2 (1), a006346.
39. Yoo, K., Park, S., Terpenoids as potential anti-alzheimer's disease therapeutics. Molecules 17 (2012), 3524–3538.
40. Zhang, M., Xu, Z., Ge, Y., Jiang, F., Liu, Y., Binding of fullerol to human serum albumin : Spectroscopic and electrochemical approach. J. Photochem. Photobiol. B : Biol. 108 (2012), 34–43.