Cholinesterase inhibitory activities of some flavonoid derivatives and chosen xanthone and their molecular docking studies

Chemico-Biological Interactions

Volumn 181, Issue 3, 2009, Pages 383-389

  Khan, Mahmud Tareq Hassan ^a   Orhan, I ^b   Senol F S ^b   Kartal, M ^c   Sener B ^b   Dvorska M ^d   Smejkal K ^d   Slapetova T ^d  

^a UNIVERSITY OF TROMSØ   (Norway)

^b GAZI UNIVERSITY   (Turkey)

^c ANKARA UNIVERSITY   (Turkey)

^d UNIVERSITY OF VETERINARY AND PHARMACEUTICAL SCIENCES   (Czech Republic)

Author keywords

Acetylcholinesterase; Alzheimer's disease; Butyrylcholinesterase; Flavonoids; Molecular docking; Xanthone

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; GALANTAMINE; KAEMPFEROL; KAEMPFEROL 3 GALACTOSIDE; MACLURAXANTHONE; QUERCETIN; RUTOSIDE; UNCLASSIFIED DRUG; XANTHONE DERIVATIVE;

ARTICLE; CHOLINESTERASE INHIBITION; COMPETITIVE INHIBITION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG BINDING SITE; DRUG POTENCY; DRUG STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SPECIFICITY; HYDROGEN BOND; HYDROPHOBICITY; IC 50; MOLECULAR DOCKING;

ACETYLCHOLINESTERASE; BUTYRYLCHOLINESTERASE; CHOLINESTERASE INHIBITORS; FLAVONOIDS; HUMANS; MODELS, MOLECULAR; XANTHONES;

RUMEX;

EID: 70249147178     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2009.06.024     Document Type: Article

References (31)

1. Burak M., and Çimen Y. Flavonoids and their antioxidant properties. Türkiye Klin. Tip Bil. Derg. 19 (1999) 296-304
2. Castañeda-Ovando A., Pacheco-Hernández D., Páez-Hernández E., Rodríguez J.A., and Galán-Vidal C.A. Chemical studies of anthocyanins: a review. Food Chem. 113 (2009) 859-871
3. Lee Y.K., Yuk D.Y., Lee J.W., Lee S.Y., Ha T.Y., Oh K.W., Yun Y.P., and Hong J.T. (-)-Epigallocatechin-3-gallate prevents lipopolysaccharide-induced elevation of beta-amyloid generation and memory deficiency. Brain Res. 1250 (2009) 164-174
4. Pratico D. Oxidative stress hypothesis in Alzheimer's disease: a reappraisal. Trends Pharmacol. Sci. 29 (2008) 609-615
5. Rivière C., Richard T., Vitrac X., Mérillon J.M., Valls J., and Monti J.P. New polyphenols active on β-amyloid aggregation. Bioorg. Med. Chem. Lett. 18 (2008) 828-831
6. Musial A., Bajda M., and Malawska B. Recent developments in cholinesterases inhibitors for Alzheimer's disease treatment. Curr. Med. Chem. 14 (2007) 2654-2679
7. Correa-Basurto J., Flores-Sandoval C., Marin-Cruz J., Rojo-Dominguez A., Espinoza-Fonseca L., and Trujillo-Ferrara J.G. Docking and quantum mechanic studies on cholinesterases and their inhibitors. Eur. J. Med. Chem. 42 (2007) 10-19
8. Piazzi L., Cavalli A., Belluti F., Bisi A., Gobbi S., Rizzo S., Bartolini M., Andrisano V., Recanatini M., Rampa A., and Extensive. SAR and computational studies of 3-1-6,7-dimethoxy-2H-2-chromenone (AP2238) derivatives. J. Med. Chem. 50 (2007) 4250-4254
9. Deliorman-Orhan D., Şenol F.S., Kartal M., and Orhan I. Assessment of antiradical potential of Calluna vulgaris (L.) Hull and its major flavonoid. J. Sci. Food Agric. 89 (2009) 809-814
10. Iinuma M., Tosa H., Tanaka T., and Yonemori S. Two xanthones from root bark of Calophyllum inophyllum. Photochemistry 35 (1994) 527-532
11. Ellman G.L., Courtney K.D., Andres V., and Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7 (1961) 88-95
12. Orhan I., Şener B., Choudhary M.I., and Khalid A. Acetyl cholinesterase and butyrylcholinesterase inhibitory activities of some Turkish medicinal plants. J. Ethnopharmacol. 91 (2004) 57-60
13. Orhan I., Kartal M., Naz Q., Yilmaz G., Kan Y., Konuklugil B., Şener B., and Choudhary M.I. Antioxidant and anticholinesterase evaluation of selected Turkish Salvia species. Food Chem. 103 (2007) 1247-1254
14. 50) of an enzymatic reaction. Biochem. Pharmacol. 22 (1973) 3099-3108
15. Gaucher J.F., Selkti M., Tiraboschi G., Prange T., Roques B.P., Tomas A., and Fournie-Zaluski M.C. Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases. Biochemistry 38 (1999) 12569-12576
16. Selkti M., Tomas A., Gaucher J.F., Prange T., Fournie-Zaluski M.C., Chen H., and Roques B.P. Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 1200-1205
17. Abagyan R.A., Totrov M.M., and Kuznetsov D.A. Icm: a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comp. Chem. 15 (1994) 488-506
18. Bourne Y., Grassi J., Bougis P.E., and Marchot P. Conformational flexibility of the acetylcholinesterase tetramer suggested by X-ray crystallography. J. Biol. Chem. 274 (1999) 30370-30376
19. Schapira M., Totrov M., and Abagyan R. Prediction of the binding energy for small molecules, peptides and proteins. J. Mol. Recog. 12 (1999) 177-190
20. Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
21. Decker M. Homobivalent quinazolinimines as novel nanomolar inhibitors of cholinesterases with dirigible selectivity toward butyrylcholinesterase. J. Med. Chem. 49 (2006) 5411-5413
22. Giacobini E., Spiegel R., Enz A., Veroff A.E., and Cutler N.R. Inhibition of acetyl- and butyryl-cholinesterase in the cerebrospinal fluid of patients with Alzheimer's disease by rivastigmine: correlation with cognitive benefit. J. Neural Transm. 109 (2002) 1053-1065
23. Zhang H.Y., Yang D.P., and Tang G.Y. Multipotent antioxidants: from screening to design. DDT 11 (2006) 749-754
24. Orhan I., Kartal M., Tosun F., and Şener B. Screening of various phenolic acids and flavonoid derivatives for their anticholinesterase potential. Z. Naturforsch. 62c (2007) 829-832
25. Fan P., Hay A.E., Marston A., and Hostettmann K. Acetylcholinesterase-inhibitory activity of linarin from Buddleja davidii, structure-activity relationships of related flavonoids, and chemical investigation of Buddleja nitida. Pharm. Biol. 46 (2008) 596-601
26. Gnerre C., Thull U., Gaillard P., Carrupt P.A., Testa B., Fernandes E., Silva F., Pinto M., Pinto M.M.M., Wolfender J.L., Hostettmann K., and Cruciani G. Natural and synthetic xanthones as monoamine oxidase inhibitors: biological assay and 3D-QSAR. Helv. Chim. Acta 84 (2001) 552-570
27. Brühlmann C., Marston A., Hostettman K., Carrupt P.A., and Testa B. Screening of non-alkaloidal natural compounds as acetylcholinesterase inhibitors. Chem. Biodivers. 1 (2004) 819-829
28. Dajas F., Arredondo F., Echeverry C., Ferreira M., Morquio A., and Rivera F. Flavonoids and the brain: evidences and putative mechanisms for a protective capacity. Curr. Neuropharmacol. 3 (2005) 193-205
29. Zhu J.T.T., Choi R.C.Y., Chu G.K.Y., Cheung A.W.H., Gao Q.T., Li J., Jiang Z.Y., and Tsim K.W.K. Flavonoids possess neuroprotective effects on cultured pheochromocytoma PC12 cells: a comparison of different flavonoids in activating estrogenic effect and in preventing β-amyloid-induced cell death. J. Agric. Food Chem. 55 (2007) 2438-2445
30. Ansari M.A., Abdul H.M., Joshi G., Opii W.O., and Butterfield D.A. Protective effect of quercetin in primary neurons against Aβ(1-42): relevance to Alzheimer's disease. J. Nutr. Biochem. 20 (2009) 269-275
31. Song K.S., Choi S.H., Hur J.M., Park H.J., Yang E.J., Mook-Jung I., Yi J.H., and Jun M. Inhibitory effects of flavonoids isolated from leaves of Petasites japonicus on β-secretase (BACE1). Food Sci. Biotechnol. 17 (2008) 1165-1170