Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar- and N-blocked-boroPro inhibitors of FAP, DPP4, and POP

Bioorganic and Medicinal Chemistry Letters

Volumn 17, Issue 5, 2007, Pages 1438-1442

  Tran, Thuy ^a   Quan, Clifford ^a   Edosada, Conrad Yap ^a   Mayeda, Mark ^a   Wiesmann, Christian ^a   Sutherlin, Dan ^a   Wolf, Beni B ^a  

^a GENENTECH INC   (United States)

Author keywords

BoroPro; Dipeptidyl peptidase; DPP4; FAP; POP; Prolyl peptidase

Indexed keywords

BORONIC ACID DERIVATIVE; FIBROBLAST ACTIVATION PROTEIN; PROLYL ENDOPEPTIDASE; PROLYL PEPTIDASE DIPEPTIDYL PEPTIDASE 4; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; DRUG ACTIVITY; DRUG POTENCY; DRUG SELECTIVITY; DRUG SYNTHESIS; ENZYME INHIBITION; STRUCTURE ACTIVITY RELATION;

ADENOSINE DEAMINASE; ANTIGENS, CD26; ANTIGENS, NEOPLASM; BORON COMPOUNDS; GLYCOPROTEINS; PROLINE; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR MARKERS, BIOLOGICAL;

EID: 33846904812     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2006.11.072     Document Type: Article

References (13)

1. Rosenblum J.S., and Kozarich J.W. Curr. Opin. Chem. Biol. 7 (2003) 496
2. Edosada C.Y., Quan C., Wiesmann C., Tran T., Sutherlin D., Reynolds M., Elliott J.M., Raab H., Fairbrother W., and Wolf B.B. J. Biol. Chem. 281 (2006) 7437
3. Edosada C.Y., Quan C., Tran T., Pham V., Wiesmann C., Fairbrother W., and Wolf B.B. FEBS Lett. 580 (2006) 1581
4. Coutts S.J., Kelly T.A., Snow R.J., Kennedy C.A., Barton R.W., Adams J., Krolikowski D.A., Freeman D.M., Campbell S.J., Ksiazek J.F., and Bachovchin W.W. J. Med. Chem. 39 (1996) 2087
5. Jones B., Adams S., Miller G.T., Jesson M.I., Watanabe T., and Wallner B.P. Blood 102 (2003) 1641
6. Adams S., Miller G.T., Jesson M.I., Watanabe T., Jones B., and Wallner B.P. Cancer Res. 64 (2004) 5471
7. Cheng J.D., Valianou M., Canutescu A.A., Jaffe E.K., Lee H.O., Wang H., Lai J.H., Bachovchin W.W., and Weiner L.M. Mol. Cancer Ther. 4 (2005) 351
8. Hu Y., Ma L., Wu M., Wong M.S., Li B., Corral S., Yu Z., Nomanbhoy T., Alemayehu S., Fuller S.R., Rosenblum J.S., Rozenkrants N., Minimo L.C., Ripka W.C., Szardenings A.K., Kozarich J.W., and Shreder K.R. Bioorg. Med. Chem. Lett. 15 (2005) 4239
9. Coutts S.J., Adams J., Krolikowski D.A., and Snow R.J. Tetrahedron Lett. 35 (1994)
10. m is the Michaelis constant for substrate hydrolysis. The presented values represent the average of at least three independent experiments with standard errors less than 10%.
11. Aertgeerts K., Levin A., Shi L., Snell G.P., Jennings A., Prasad G.S., Zhang Y., Kraus M.L., Salakian S., Sridhar V., Wijnands R., and Tennant M.G. J. Biol. Chem. 280 (2005) 19441
12. Engel M., Hoffmann T., Manhart S., Heiser U., Chambre S., Huber R., Demuth H., and Bode W. J. Mol. Biol. 355 (2006) 768
13. Fulop V., Bocskei Z., and Polgar L. Cell 94 (1998) 161