A new series of 3-phenylcoumarins as potent and selective MAO-B inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 12, 2009, Pages 3268-3270

  Matos, Maria Joao ^a,b   Viña, Dolores ^a   Quezada, Elias ^a,b   Picciau, Carmen ^b   Delogu, Giovanna ^b   Orallo, Francisco ^a   Santana, Lourdes ^a   Uriarte, Eugenio ^a  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

^b Dipartimento di Scienze Mediche Facolta di Medicina   (Italy)

Author keywords

3 Phenylcoumarins; Coumarin; Monoamino oxidase inhibitors; Perkin reaction; Resveratrol

Indexed keywords

3 (3',5' DIMETHOXY)PHENYL 6 METHYLCOUMARIN; 3 (4' METHOXY)PHENYL 6 METHYLCOUMARIN; 3 PHENYLCOUMARIN DERIVATIVE; 6 METHYL 3 (3',4',5' TRIMETHOXY)PHENYLCOUMARIN; 6 METHYL 3 PHENYLCOUMARIN; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; BENZENE DERIVATIVE; COUMARIN DERIVATIVE; IPRONIAZID; MONOAMINE OXIDASE A INHIBITOR; MONOAMINE OXIDASE B INHIBITOR; PHENYLACETIC ACID; RESVERATROL; SALICYLALDEHYDE; SELEGILINE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION; DRUG DESIGN; DRUG POTENCY; DRUG SCREENING; DRUG SELECTIVITY; DRUG SYNTHESIS; ENZYME INHIBITION; IC 50; PERKIN REACTION; QUANTUM YIELD;

ANTIOXIDANTS; COUMARINS; DRUG DESIGN; HUMANS; INHIBITORY CONCENTRATION 50; MONOAMINE OXIDASE; MONOAMINE OXIDASE INHIBITORS; SELEGILINE; STILBENES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 65749116833     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.04.085     Document Type: Article

References (35)

1. Borges F., Roleira F., Milhazes N., Santana L., and Uriarte E. Curr. Med. Chem. 12 (2005) 887
2. Hoult J.R.S., and Payá M. Gen. Pharmacol. 27 (1996) 713
3. Kontogiorgis C., and Hadjipavlou-Litina D. J. Enzyme Inhib. Med. Chem. 18 (2003) 63
4. Kabeya L., Marchi A., Kanashiro A., Lopes N., Silva C., Pupo M., and Lucisano-Valim Y. Bioorg. Med. Chem. 15 (2007) 1516
5. Carotti A., Altomare C., Catto M., Gnerre C., Summo L., De Marco A., Rose S., Jenner P., and Testa B. Chem. Biod. 3 (2006) 134
6. Chilin A., Battistutta R., Bortolato A., Cozza G., Zanatta S., Poletto G., Mazzorana M., Zagotto G., Uriarte E., Guiotto A., Pinna L., Meggio F., and Moro S. J. Med. Chem. 51 (2008) 752
7. Santana L., Uriarte E., González-Díaz H., Zagotto G., Soto-Otero R., and Méndez-Álvarez E. J. Med. Chem. 49 (2006) 1118
8. Santana L., González-díaz H., Quezada E., Uriarte E., Yáñez M., Viña D., and Orallo F. J. Med. Chem. 51 (2008) 6740
9. Catto M., Nicolotti O., Leonetti F., Carotti A., Favia A., Soto-Otero R., Méndez-Álvarez E., and Carotti A. J. Med. Chem. 49 (2006) 4912
10. Gnerre C., Catto M., Leonetti F., Weber P., Carrupt P., Altomare C., Carotti A., and Testa B. J. Med. Chem. 43 (2000) 4747
11. Chimenti F., Secci D., Bolasco A., Chimenti P., Granese A., Befani O., Turini P., Alacaro S., and Ortuso F. Bioorg. Med. Chem. Lett. 14 (2004) 3697
12. Frémont L. Life Sci. 66 (2000) 663
13. Orallo F. In: Aggarwal B.B., and Shishodia S. (Eds). Resveratrol in Health and Disease (2005), CRC Press, USA 577
14. Leiro J., Álvarez E., Arranz J., Laguna R., Uriarte E., and Orallo F. J. Leukocyte Biol. 75 (2004) 1156
15. Orallo F. Curr. Med. Chem. 15 (2008) 1887
16. Yánez M., Fraiz N., Cano E., and Orallo F. Biochem. Biophys. Res. Commun. 344 (2006) 688
17. Vilar S., Quezada E., Santana L., Uriarte E., Yánez M., Fraiz N., Alcaide C., Cano E., and Orallo F. Bioorg. Med. Chem. Lett. 16 (2006) 257
18. Vilar S., Quezada E., Alcaide C., Orallo F., Santana L., and Uriarte E. Qsar Comb. Sci. 26 (2007) 317
19. De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., and Mattevi A. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 12684
20. Grimsby J., Lan N.C., Neve R., Chen K., and Shih J.C. J. Neurochem. 55 (1990) 1166
21. Edmondson D.E., Mattevi A., Binda C., Li M., and Hubalek F. Curr. Med. Chem. 11 (2004) 1983
22. Harfenist H., Heuseur D.J., Joyner C.T., Batchelor J.F., and White H.L. J. Med. Chem. 39 (1996) 1857
23. Wouters J. Curr. Med. Chem. 5 (1998) 137
24. Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., and Mattevi A. Nat. Struct. Biol. 9 (2002) 22
25. Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., and Mattevi A. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 9750
26. Ma J., Yoshimura M., Yamashita E., Nakagawa A., Ito A., and Tsukihara T. J. Mol. Biol. 338 (2004) 103
27. Hans N., Singhi M., Sharma V., and Grover S.K. Indian J. Chem., Sect. B 35 (1996) 1159
28. Mohanty S., Makrandi J.K., and Grover S.K. Indian J. Chem., Sect. B 28 (1989) 766
29. Kamat S.P., D́Souza A.M., Paknikar S.K., and Beaucahmp P.S. J. Chem. Res. (S) (2002) 242
30. 2: C, 81.34; H, 5.12; O, 13.54. Found: C, 81.44; H, 4.84.
31. 3: C, 76.68; H, 5.30; O, 18.02. Found: C, 76.88; H, 5.32.
32. 4: C, 72.96; H, 5.44; O, 21.60. Found: C, 73.23; H, 4.90.
33. 5: C, 69.93; H, 5.56; O, 24.51. Found: C, 70.14; H, 5.58.
34. ® Red reagent in a sodium phosphate buffer.The specific fluorescence emission (used to obtain the final results) was calculated after subtraction of the background activity, which was determined from vials containing all components except the hMAO isoforms, which were replaced by a sodium phosphate buffer solution.On the other hand, in our experiments and under our experimental conditions, the control activity of hMAO-A and hMAO-B (using p-tyramine as a common substrate for both isoforms) was 165 ± 2 pmol of p-tyramine oxidized to p-hydroxyphenylacetaldehyde/min (n = 20).
35. 50 values shown in the table are expressed as means ± SEM from five experiments.