Using peptidic inhibitors to systematically probe the S1′ site of caspase-3 and caspase-7

Organic Letters

Volumn 7, Issue 16, 2005, Pages 3529-3532

  Goode, David R ^a   Sharma, Anil K ^a   Hergenrother, Paul J ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL ASPARTYL GLUTAMYL VALYL ASPARTAL; ACETYL-ASPARTYL-GLUTAMYL-VALYL-ASPARTAL; CASPASE; CASPASE 3; CASPASE 7; ENZYME INHIBITOR; OLIGOPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMBINATORIAL CHEMISTRY; DRUG ANTAGONISM; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

AMINO ACID SEQUENCE; CASPASE 3; CASPASE 7; CASPASES; COMBINATORIAL CHEMISTRY TECHNIQUES; ENZYME INHIBITORS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OLIGOPEPTIDES; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 23944461510     PISSN: 15237060     EISSN: None     Source Type: Journal    
DOI: 10.1021/ol051287d     Document Type: Article

References (30)

1. For reviews on caspases, see: (a) Denault, J. B.; Salvesen, G. S. Chem. Rev. 2002, 102, 4489-4500.
2. (b) Nicholson, D. W. Cell Death Diff. 1999, 6, 1028-1042.
3. (c) Fuentes-Prior, P.; Salvesen, G. S. Biochem. J. 2004, 384, 201-232.
4. For reviews on caspase inhibition, see: (a) Wang, K. K. W. Curr. Opin. Drug Discovery Dev. 1999, 2, 519-527.
5. (b) Talanian, R. V.; Brady, K. D.; Cryns, V. L. J. Med. Chem. 2000, 43, 3351-3371.
6. (c) Concha, N. O.; Abdel-Meguid, S. S. Curr. Med. Chem. 2002, 9, 713-726.
7. P denotes substrate position, and S denotes enzyme site or pocket.
8. Thornberry, N. A.; Rano, T. A.; Peterson, E. P.; Rasper, D. M.; Timkey, T.; Garcia-Calvo, M.; Houtzager, V. M.; Nordstrom, P. A.; Roy, S.; Vaillancourt, J. P.; Chapman, K. T.; Nicholson, D. W. J. Biol. Chem. 1997, 272, 17907-17911.
9. Although their substrate specificities are different from the ones listed, on the basis of the length of their propeptide domains, caspase-6 is often placed in Group II, and caspase-2 is generally placed in group III. See: Shi, Y. Mol Cell 2002, 9, 459-470.
10. Caspase-1 has also been implicated in the apoptotic pathway. See: Choi, C.; Jeong, E.; Benveniste, E. N. J. Neurooncol. 2004, 67, 167-176.
11. (a) Talanian, R. V.; Quinlan, C.; Trautz, S.; Hackett, M. C.; Mankovich, J. A.; Banach, D.; Ghayur, T.; Brady, K. D.; Wong, W. W. J. Biol. Chem. 1997, 272, 9677-9682.
12. (b) Chereau, D.; Kodandapani, L.; Tomaselli, K. J.; Spada, A. P.; Wu, J. C. Biochemistry 2003, 42, 4151-4160.
13. (a) Han, Y.; Giroux, A.; Grimm, E. L.; Aspiotis, R.; Francoeur, S.; Bayly, C. I.; Mckay, D. J.; Roy, S.; Xanthoudakis, S.; Vaillancourt, J. P.; Rasper, D. M.; Tam, J.; Tawa, P.; Thornbeny, N. A.; Paterson, E. P.; Garcia-Calvo, M.; Becker, J. W.; Rotonda, J.; Nicholson, D. W.; Zamboni, R. J. Bioorg. Med. Chem. Lett. 2004, 14, 805-808.
14. (b) Han, Y.; Giroux, A.; Colucci, J.; Bayly, C. I.; Mckay, D. J.; Roy, S.; Xanthoudakis, S.; Vaillancourt, J.; Rasper, D. M.; Tam, J.; Tawa, P.; Nicholson, D. W.; Zamboni, R. J. Bioorg. Med. Chem. Lett. 2005, 15, 1173-1180.
15. For the effect of substitution in the P1′ position on the inhibition of caspase-1, see: (a) Mjalli, A. M. M.; Chapman, K. T.; MacCoss, M.; Thornberry, N. A. Bioorg. Med. Chem. Lett. 1993, 3, 2689-2692.
16. (b) Mjalli, A. M. M.; Chapman, K. T.; MacCoss, M. Bioorg. Med. Chem. Lett. 1993, 3, 2693-2698.
17. Becker, J. W.; Rotonda, J.; Soisson, S. M.; Aspiotis, R.; Bayly, C.; Francoeur, S.; Gallant, M.; Garcia-Calvo, M.; Giroux, A.; Grimm, E.; Han, Y.; McKay, D.; Nicholson, D. W.; Peterson, E.; Renaud, J.; Roy, S.; Thornberry, N.; Zamboni, R. J. Med. Chem. 2004, 47, 2466-2474.
18. Brady, K. D.; Giegel, D. A.; Grinnell, C.; Lunney, E.; Talanian, R. V.; Wong, W.; Walker, N. Bioorg. Med. Chem. 1999, 7, 621-631.
19. Rotonda, J.; Nicholson, D. W.; Fazil, K. M.; Gallant, M.; Gareau, Y.; Labelle, M.; Peterson, E. P.; Rasper, D. M.; Ruel, R.; Vaillancourt, J. P.; Thornbeny, N. A.; Becker, J. W. Nat. Struct. Biol. 1996, 3, 619-625.
20. Wei, Y.; Fox, T.; Chambers, S. P.; Sintchak, J.; Coll, J. T.; Golec, J. M.; Swenson, L.; Wilson, K. P. Charifson, P. S. Chem. Biol. 2000, 7, 423-432.
21. (a) Hoeg-Jensen, T.; Jakobsen, M. H.; Holm, A. Tetrahedron Lett. 1991, 32, 6387-6390.
22. (b) Carpino, L. A.; Ghassemi, S.; Ionescu, D.; Ismail, M.; Sadat-Aalaee, D.; Truran, G. A.; Mansour, E. M. E.; Siwrak, G. A.; Eynon, J. S.; Morgan, B. Org. Process Res. Dev. 2003, 7, 28-37.
23. Sharma, A. K.; Hergenrother, P. J. Org. Lett. 2003, 5, 2107-2109.
24. Vazquez, J.; Albericio, F Tetrahedron Lett. 2002, 43, 7499-7502.
25. Stennicke, H. R.; Salvesen, G. S. Methods 1999, 17, 313-319.
26. M)).
27. (a) Allen, D. A.; Pham, P.; Choong, I. C.; Fahr, B.; Burdett, M. T.; Lew, W.; DeLano, W. L.; Gordon, E. M.; Lam, J. W.; O'Brien, T.; Lee, D. Bioorg. Med. Chem. Lett. 2003, 13, 3651-3655.
28. (b) Choong, I. C.; Lew, W.; Lee, D.; Pham, P.; Burdett, M. T.; Lam, J. W.; Wiesmann, C.; Luong, T. N.; Fahr, B.; DeLano, W. L.; McDowell, R. S.; Allen, D. A.; Erlanson, D. A.; Gordon, E. M.; O'Brien, T. J. Med. Chem. 2002, 45, 5005-5022.
29. Modeling studies were performed using the MOE software package, and visualization was carried out using MOLCAD. (a) MOE version 2004, Chemical Computing Group, Montreal, 2004.
30. (b) SYBYL 7.0, Tripos Inc., St. Louis, Missouri, 2004.