Discovery of a novel series of potent and selective substrate-based inhibitors of p60(c-src) protein tyrosine kinase: Conformational and topographical constraints in peptide design

Journal of Medicinal Chemistry

Volumn 41, Issue 13, 1998, Pages 2252-2260

  Alfaro Lopez, Josue ^a   Yuan, Wei ^a   Phan, Brigitte C ^b   Kamath, Jayesh ^b   Lou, Qiang ^b   Lam, Kit S ^b   Hruby, Victor J ^a  

^a University of Arizona   (United States)

^b UNIVERSITY OF ARIZONA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

N ALPHA FLUORENYLMETHOXYCARBONYL BETA METHYL 2' NAPHTHYLALANINE; PROTEIN TYROSINE KINASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; DRUG CONFORMATION; DRUG POTENCY; DRUG SPECIFICITY; DRUG SYNTHESIS; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SPECIFICITY; STEREOISOMERISM; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; DRUG DESIGN; ENZYME INHIBITORS; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; ONCOGENE PROTEIN PP60(V-SRC); PHOSPHORYLATION; PROTEIN CONFORMATION; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0032543527     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9707885     Document Type: Article

References (61)

1. (a) Zhow, S.; Carraway, K. L.; Eck, M. J.; Cantley, L. C. Catalytic specificity of protein-tyrosine kinases is critical for selective signaling. Nature 1995, 373, 536-539.
2. c-src family of protein tyrosine kinases. int. J. Biochem. Cell Biol. 1995, 27, 551-563.
3. (c) Davis, R. J. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 1993, 268, 14553-14556.
4. (d) Zhow, S.; Shoelson, S. E.; Chauduri, M.; Pawson, T.; Fajardo, J. E. SH2 domains recognize specific phosphopeptide sequences. Cell 1993, 72, 767-778.
5. Ottenhoff-Kalf, A. E.; Rijksen, G.; Van Beurden, E. A.; Steal, G. E. Characterization of protein tyrosine kinases from human breast cancer. involvement of the c-Src oncogene product. Cancer Res. 1992, 52, 4773-4778.
6. Levitzki, A. Signal transduction theraphy- A novel approach to disease managment. Eur. J. Biochem. 1994, 226, 1-13.
7. (a) Resh, M. D. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 1994, 76, 411-413.
8. (b) Howell, J. A. The when and how of Src regulation. Cell 1993, 73, 1051-1054.
9. Xu, W.; Harrison, S. C.; Eck, M. J. Three-dimensional structure of tyrosine kinase c-Src. Nature 1997, 385, 595-601.
10. Van Der Geer, P.; Hunter, T.; Lindberg, R. A. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell. Biol. 1994, 10, 251-337.
11. (a) Aaronson, S. A. Growth factors and cancer. Science 1991, 254, 1146-1153.
12. (b) Cantley, L. C.; Auger, K. R.; Carbenter, C.; Graziani, A.; Soltoff, S. Oncogenes and signal transduction. Cell 1991, 64, 281-302.
13. (c) Ullrich, A.; Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61, 203-212.
14. Marx, J. Oncogenes evoke new cancer therapies. Science 1990, 249, 1376-1378.
15. (a) Levitzki, A.; Gazit, A. Tyrosine Kinase inhibition: An Approach to Drug Development. Science 1995, 267, 1782-1788.
16. (b) Langdon, S. P.; Smith, G. F. inhibition of cell signaling pathways. Cancer Treat. Rev. 1995, 21, 65-89.
17. Elder, J. E.; Fisher, G. J.; Lindquist, P. B.; Voorthees, J. J.; Coffey, R. J., Jr. Overexpression of transforming growth factor α in psoriatic epidermis. Science 1989, 243, 811-814.
18. Hajjar, D. P.; Pomerants, H. B. Signal transduction in athero-sclerosis: integration of cytokines and the eicosanoidnetwork. FASEB J. 1992, 6, 2933-2941.
19. Libby, P.; Schwartz, D.; Borgie, E.; Tanaka, H. A cascade model for restenosis as special case of atherosclerosis progression. Circulation 1992, 86, 47-52.
20. (a) Fry, W. D. Recent advances in tyrosine kinase inhibitors. Annu. Rep. Med. Chem. 1996, 31, 151-160.
21. (b) Boutin, J. A. Tyrosine protein kinase inhibition and cancer. int. J. Biochem. 1994, 26, 1203-1226.
22. (c) Burke, T. R., Jr. Protein-tyrosine kinases: potential targets for anticancer drug development. Stem Cells 1994, 12, 1-6.
23. (d) Levitzki, A. Tyrophostins: tyrosine kinase blockers as novel antiproliferative agents and dissectors of signal transduction. FASEB J. 1992, 6, 3275-3282.
24. (e) Burke, T. R., Jr. Protein-tyrosine kinase inhibitors. Drugs Future 1992, 17, 19-131.
25. (f) Chang, C. J.; Geahlen, R. L. Protein-tyrosine kinase inhibition: mechanism-based discovery of antitumor agents. J. Nat. Prod. 1992, 55, 1529-1560.
26. (a) Eckhart, W.; Hutchinson, M. A.; Hunter, T. An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates. Cell 1979, 18, 925-933.
27. (b) Courtneidge, S. A.; Smith, A. E. Polyoma virus transforming protein associates with the product of the c-src cellular gene. Nature 1983, 303, 435-439.
28. (c) Taylor, S. J.; Shaollowai, P. The cell cycle and c-Src. Curr. Opin. Genet. Dev. 1993, 3, 26-34.
29. c-src in progessive stages of human colorectal cancer. J. Clin. invest. 1993, 91, 53-60.
30. (b) Talamonti, M. S.; Curley, S. A.; Gallick, G. E. Development and progression of human colon cancer. Cancer Bull. 1992, 44, 321-326.
31. c-src protein kinase is an early event in colonic carcino-genesis. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 558-562.
32. (d) Guy, C. T.; Muthuswamy, S. K.; Cardiff, R. D.; Soriano, P. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev. 1994, 8, 23-32.
33. c-src with two major signaling pathways in human breast cancer. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 83-87.
34. (f) Lynch, S. A.; Bfrugge, J. S.; Fromowitz, F.; Glantz, L.; Viola, M. V. increased expression of the src proto-oncogene in hairy cell leukemia and a subgroup of B-cell limphomas. Leukemia 1993, 7, 1416-1422.
35. (a) Dow, R. L.; Chow, T. T.; Bechle, B. M.; Larson, E. R. Identification of tricyclic analogues related to ellagic acid as potent/selective tyrosine protein kinase inhibitors. J. Med. Chem. 1994, 31, 2221-2231.
36. c-src. Bioorg. Med. Chem. Lett. 1995, 5, 2423-2428.
37. Traut, T. W. intracellular concentrations of ATP can be as high as 5 μM. Mol. Cell Biochem. 1994, 140, 1-22.
38. c-src. J. Med. Chem. 1995, 38, 4276-4283.
39. (a) Houghten, R. A.; Pinilla, C.; Blondelle, S. E.; Cuervo, J. H. Generation and use of synthetic peptide libaries for basic research and drug discovery. Nature 1991, 354, 84-86.
40. (b) Cwirla, S. E.; Peters, E. A.; Barret, R. W.; Dower, W. J. Peptides on phage: a vast library of peptides for identifying ligands. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 6378-6382.
41. Lam, K. S.; Salmon, S. E.; Hersh, E. M.; Hruby, V. J.; Kazmiersky, W. M.; Knapp, R. J. A new type of synthetic peptide library for identifying ligand-binding activity. Nature 1991, 354, 82-84.
42. Lam, K. S.; Wu, J.; Lou, Q. Identification and characterization of a novel synthetic peptide substrate specific for Src-family protein tyrosine kinases. int. J. Pept. Protein Res. 1995, 45, 587-592.
43. c-src protein tyrosine kinase. Lett. Pept. Sci. 1995, 2, 286-289.
44. Yuan, W.; Hruby, V. J. Asymmetric synthesis of unusual amino acids: Synthesis of four isomers of β-methyl-3-(2′-naphthyl)-alanine. Tetrahedron Lett. 1997, 38, 5853-5856.
45. Ball, J. R.; Hughes, R. A. β-turn topography. Tetrahedron 1993, 49, 3467-3478.
46. c-src protein tyrosine kinase. Lett. Pept. Sci. 1996, 3, 309-316.
47. Lou, Q.; Wu, J.; Lam, K. S. A protein kinase assay for both acidic and basic peptides. Anal. Biochem. 1996, 235, 107-109.
48. Mosberg, H. I.; Hurst, T.; Hruby, V. J.; Yamamura, H. I. Bispenicillamine enkephalins possess highly improved specificity toward δ opiod receptors. Proc. Natl. Acad. Sci. U.S.A. 1983, 80, 5871-5874.
49. Hruby, V. J.; Boteju, L. W. Peptides and mimics, design of conformationally constrained. In Encyclopedia of Molecular Biology and Molecular Medicine; Meyers, R. A., Ed.; VCH: Weinheim, 1996; Vol. 4, pp 371-382.
50. Hruby, V. J.; Li, G.; Haskell-Luevano, C.; Shenderovich, M. Design of peptides, proteins and peptidomimetics in chi space. Biopolymers 1997, 43, 219-266.
51. (a) Qian, X.; Kövér, K. E.; Shenderovich, M. D.; Hruby, V. J. Probing the stereochemical requirements for receptor recognition of δ-opioid agonists through topographic modifications in position 1. J. Am. Chem. Soc. 1996, 775, 7282-7290.
52. (b) Haskell-Luevano, C.; Boteju, L. W.; Miwa, H.; Hadley, M. E.; Gantz, I.; Hruby, V. J. Topographical modification of melanotropin peptide analogues with β-methyltryptophan isomers at position 9 leads to differential potencies and prolonged biological activities. J. Med. Chem. 1995, 38, 4720-4729.
53. (c) Azizeh, B. Y.; Shenderovich, M. D.; Trivedi, D.; Li, G.; Sturm, N. S.; Hruby, V. J. Topographical amino acid substitution in position 10 of glucagon analogues leads to antagonists/partial agonists with greater binding differences. J. Med. Chem. 1996, 39, 2449-2455.
54. (a) Kövér, K. E.; Jiao, D.; Fang, S.; Hruby, V. J. Conformational analysis of four β-methylphenylalanine stereoisomers in a bioactive peptide by z-filtered relay NMR. Magn. Reson. Chem. 1993, 31, 1072-1076.
55. 5]enkephalin by NMR spectroscopy and conformational energy calculations. Biopolymers 1996, 38, 141-156.
56. c-src. J. Biol. Chem. 1995, 270, 5375-5380.
57. s-src. J. Am. Chem. Soc. 1997, 119, 3844-3845.
58. s-src protein tyrosine kinase. Cancer Res. 1997, 57, 1877-1881.
59. Cheng, H. C.; Matsura, I.; Wang, J. H. in Vitro substrate specificity of protein tyrosine kinases. Mol. Cell. Biochem. 1993, 127, 103-113.
60. Kaiser, E.; Colescott, R. L.; Bossinger, C. D.; Cook, P. J. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970, 34, 595-598.
61. Misicka, A.; Hruby, V. J. Optimization of disulfide bond formation. Polish J. Chem. 1994, 68, 893-899.