Inhibition of monoamine oxidases by coumarin-3-acyl derivatives: Biological activity and computational study

Bioorganic and Medicinal Chemistry Letters

Volumn 14, Issue 14, 2004, Pages 3697-3703

  Chimenti, Franco ^a   Secci, Daniela ^a   Bolasco, Adriana ^a   Chimenti, Paola ^a   Granese, Arianna ^a   Befani, Olivia ^a   Turini, Paola ^a   Alcaro, Stefano ^b   Ortuso, Francesco ^b  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY MAGNA GRAECIA OF CATANZARO   (Italy)

Author keywords

Coumarin; MAO inhibitors

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); BROFAROMINE; CARBOXYLIC ACID DERIVATIVE; CHLORIDE; COUMARIN DERIVATIVE; IPRONIAZID; ISOENZYME; LU 53439; MOCLOBEMIDE; MONOAMINE OXIDASE INHIBITOR; PARGYLINE; SELEGILINE; TOLOXATONE; UNCLASSIFIED DRUG;

ARTICLE; DRUG ACTIVITY; DRUG RESEARCH; DRUG SELECTIVITY; DRUG SYNTHESIS; ENZYME INHIBITION; IC 50; MATHEMATICAL COMPUTING; MOLECULAR INTERACTION;

AMINE OXIDASE (COPPER-CONTAINING); ANIMALS; BINDING SITES; BRAIN; CELL LINE; COMPUTATIONAL BIOLOGY; COUMARINS; INHIBITORY CONCENTRATION 50; MOLECULAR CONFORMATION; MONOAMINE OXIDASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP;

STAPHYLOCOCCUS PHAGE 3A;

EID: 2942527408     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2004.05.010     Document Type: Article

References (43)

1. Greenawalt J.W., Schnaitman C. J. Cell Biol. 46:1970;173
2. Mondovì B. Structure and Function of Amine Oxidases. 1985;CRC, Boca Raton, FL
3. Johnston J.P. Biochem. Pharmacol. 17:1968;1285
4. Weyler W., Hsu Y.P., Breakefield O. Pharmacol. Ther. 47:1990;391
5. Westlund R.N., Denney R.M., Kochersperger L.M., Rose R.M., Abell C.W. Science. 219:1983;979
6. Geha R.M., Rebrin I., Chen K., Shih J.C. J. Biol. Chem. 276:2001;9877
7. Anderson M.C., Hasan F., McCrodden J.M. Neurochem. Res. 18:1993;1145
8. Wouters J. Curr. Med. Chem. 5:1998;137
9. Chiba K., Trevor A., Castagnoli N. Biochem. Biophys. Res. Commun. 120:1984;574
10. Fritz R.R., Abell C.W., Patel N.T., Gessner W., Brossi A. FEBS Lett. 186:1985;224
11. Grimsby J., Toth M., Chen K., Kumazawa T., Klaidman L., Adams J.D., Karoum F., Gal J., Shih J.C. Nat. Genet. 17:1997;1
12. De Zutter G.S., Davis R.J. Proc. Natl. Acad. Sci. U.S.A. 98:2001;6168
13. Mc Millan, et al. J. Am. Pharm. Assoc., Sci. Ed. 42:1953;457
14. Fowler C.J., Oreland L., Callingham B.A. J. Pharm. Pharmacol. 33:1981;341
15. Knoll J., Ecsery Z., Kelemen K., Nievel J., Knoll B. Arch. Int. Pharmachodyn. Ther. 155:1965;154
16. Moureau F., Wouters J., Vercauteren D.P., Collin S., Evrard G., Durant F., Ducrey F., Koenig J.J., Jarreau F.X. Eur. J. Med. Chem. 27:1992;939
17. Moureau F., Wouters J., Vercauteren D.P., Collin S., Evrard G., Durant F., Ducrey F., Koenig J.J., Jarreau F.X. Eur. J. Med. Chem. 29:1994;269
18. Moureau F., Wouters J., Depas M., Vercauteren D.P., Durant F., Ducrey F., Koenig J.J., Jarreau F.X. Eur. J. Med. Chem. 30:1995;823
19. Rabasseda X., Sorbera L.A., Castaner J. Drugs Future. 24:1999;1057
20. Wouters J., Moureau F., Evrard G., Koenig J.J., Jegham S., George P., Durant F. Bioorg. Med. Chem. 7:1999;1683
21. Bergström M., Westerberg G., Nemeth G., Traut M., Gross G., Greger G., Müller-Peltzer H., Safer A., Eckernäs S.A., Grahner A., Langström B. Eur. J. Clin. Pharm. 52:1997;121
22. Loscher W., Lehmann H., Teschendorf H.J., Traut M., Gross G. J. Pharm. Exper. Therap. 288:1999;984
23. Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A. Nat. Struct. Biol. 9:2002;22
24. Gnerre C., Catto M., Leonetti F., Weber P., Carrupt P.A., Altomare C., Carotti A., Testa B. J. Med. Chem. 43:2000;4747
25. Manna F., Chimenti F., Bolasco A., Secci D., Bizzarri B., Befani O., Turini P., Mondovi B., Alcaro S., Tafi A. Bioorg. Med. Chem. Lett. 12:2002;3629
26. Jitendra R.H., Susheel J.N., Manikrao M.S. Tetrahedron Lett. 43:2002;1127
27. Bonsignore L., De Logu A., Lavagna S.M., Loy G., Secci D. Eur. J. Med. Chem. 29:1994;479
28. Pochet L., Doucet C., Schynts M., Thierry N., Boggetto N., Pirotte B., Jiang K.Y., Masereel B., de Tullio P. J. Med. Chem. 39:1996;2579
29. Doucet C., Pochet L., Thierry N., Pirotte B., Delarge J., Reboud-Ravaux M. J. Med. Chem. 42:1999;4161
30. Bonsignore L., Cottiglia F., Lavagna S.M., Loy G., Secci D. Heterocycles. 50:1999;469
31. Ji M., Hua W., Wu X., Duan T. Zhongguo Yaoke Daxue Xuebao. 19:1988;241
32. Bonsignore L., Cottiglia F., Lavagna S.M., Loy G., Secci D. Il Farmaco. 53:1998;693. and references cited therein
33. -3 μM.
34. Basford R.E. Methods Enzymol. 10:1967;96
35. Matsumoto T., Suzuki O., Furuta T., Asai M., Kurokawa Y., Rimura Y., Katsumata Y., Takahashi I. Clin. Biochem. 18:1985;126
36. Bradford M.M. Anal. Biochem. 72:1976;248
37. Dragon ver. 3.0, 2003, Talete s.r.l., Milan, Italy
38. ClogP ver 4.81, 2003, Daylight Chemical Information Systems, Inc. Mission Viejo, 92691 California, USA
39. Alcaro S., Gasparrini F., Incani O., Mecucci S., Misiti D., Pierini M., Villani C. J. Comput. Chem. 21:2000;515-530
40. Still W.C., Tempczyk A., Hawley R.C., Hendrickson T. J. Am. Chem. Soc. 112:1990;6127
41. Macromodel Linux ver. 7.2 Mohamadi F., Richards N.G.J., Guida W.C., Liskamp R., Lipton M., Caufield C., Chang G., Hendrickson T., Still W.C. J. Comput. Chem. 11:1990;440-467
42. According to the MOLINE methodology and previously reported enzyme-ligand docking experiments, both grid resolution GR and Van der Waals compression factor χ were established at 6 and 0.8, respectively. The adopted resolution generated exactly 65, 712 configurations for each inhibitor-enzyme complex. Other docking protocol details are the activation of the selection module: SEL_5FD, and the number of cycles of the rigid optimization process: 3, each with 100 Simplex iterations. The force field used for the protocol validation was AMBER* united atoms with dielectric constant 80
43. In the constrained protocol two different shells of atoms were generated. One included all atoms located between 10 and 12 Å from FAD N5, on which a constant force of 100 kJ/mol was applied to the coordinates in order to limit the freedom of moments. The other shell included the enzyme atoms 'frozen' (rigidly fixed and not considered in the energy evaluation) more than 12 Å from the isoalloxazine moiety