Homology modeling and site-directed mutagenesis to identify selective inhibitors of endothelin-converting enzyme-2

Journal of Medicinal Chemistry

Volumn 51, Issue 12, 2008, Pages 3378-3387

  Gagnidze, Khatuna ^a   Sachchidanand, ^a,b   Rozenfeld, Raphael ^a   Mezei, Mihaly ^a   Zhou, Ming Ming ^a   Devi, Lakshmi A ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b INSTITUTE OF LIFE SCIENCES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ENDOTHELIN CONVERTING ENZYME; ENDOTHELIN CONVERTING ENZYME 2; ENDOTHELIN CONVERTING ENZYME INHIBITOR; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; NEUROPEPTIDE; PRODYNORPHIN; PROENKEPHALIN; TRYPTOPHAN; TYROSINE;

ACIDITY; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SPECIFICITY; GENE MUTATION; MOLECULAR LIBRARY; MOLECULAR MODEL; NEUROSECRETORY CELL; PH; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; GLYCOPEPTIDES; KINETICS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEPRILYSIN; PROTEIN CONFORMATION; QUINOLINES; QUINOXALINES; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SMALL MOLECULE LIBRARIES; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN; TYROSINE;

EID: 45749124056     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm7015478     Document Type: Article

References (49)

1. Docherty, K.; Steiner, D. F. Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 1982, 44, 625-638.
2. Steiner, D. F. The proprotein convertases. Curr. Opin. Chem. Biol. 1998, 2 (1), 31-39.
3. Mizuno, K.; Minamino, N.; Kangawa, K.; Matsuo, H. A new family of endogenous "big" Met-enkephalins from bovine adrenal medulla: purification and structure of docosa- (BAM-22P) and eicosapeptide (BAM-20P) with very potent opiate activity. Biochem. Biophys. Res. Commun. 1980, 97 (4), 1283-1290.
4. Yang, H. Y.; Fratta, W.; Majane, E. A.; Costa, E. Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine. Proc. Natl. Acad. Sci. U.S.A. 1985, 82 (22), 7757-7761.
5. Sigafoos, J.; Chestnut, W. G.; Merrill, B. M.; Taylor, L. C.; Diliberto, E. J., Jr.; Viveros, O. H. Novel peptides from adrenomedullary chromaffin vesicles. J. Anat. 1993, 183 (Part 2), 253-264.
6. Che, F. Y.; Yan, L.; Li, H.; Mzhavia, N.; Devi, L. A.; Fricker, L. D. Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) mice. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (17), 9971-9976.
7. Perry, S. J.; Yi-Kung Huang, E.; Cronk, D.; Bagust, J.; Sharma, R.; Walker, R. J.; Wilson, S.; Burke, J. F. A human gene encoding morphine modulating peptides related to NPFF and FMRFamide. FEBS Lett. 1997, 409 (3), 426-430.
8. Vilim, F. S.; Aarnisalo, A. A.; Nieminen, M. L.; Lintunen, M.; Karlstedt, K.; Kontinen, V. K.; Kalso, E.; States, B.; Panula, P.; Ziff, E. Gene for pain modulatory neuropeptide NPFF: induction in spinal cord by noxious stimuli. Mol. Pharmacol. 1999, 55 (5), 804-811.
9. Ahn, K. In Handbook of Proteolytic Enzymes; Academic Press: San Diego, CA, 1998; pp 1085-1089.
10. Molineaux, C.; Wilk, S. Extracellular Processing of Peptides; CRC Press: Boca Raton, FL, 1991; Chapter 10, pp 251-282.
11. Oefner, C.; D'Arcy, A.; Hennig, M.; Winkler, F. K.; Dale, G. E. Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon. J. Mol. Biol. 2000, 296 (2), 341-349.
12. Emoto, N.; Yanagisawa, M. Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 1995, 270 (25), 15262-15268.
13. Turner, A. J.; Murphy, L. J. Molecular pharmacology of endothelin converting enzymes. Biochem. Pharmacol. 1996, 51 (2), 91-102.
14. Turner, A. J.; Isaac, R. E.; Coates, D. The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. BioEssays 2001, 23 (3), 261-269.
15. Xu, D.; Emoto, N.; Giaid, A.; Slaughter, C.; Kaw, S.; deWit, D.; Yanagisawa, M. ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 1994, 78 (3), 473-485.
16. Eckman, E. A.; Reed, D. K.; Eckman, C. B. Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme. J. Biol. Chem. 2001, 276 (27), 24540-24548.
17. Eckman, E. A.; Watson, M.; Marlow, L.; Sambamurti, K.; Eckman, C. B. Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J. Biol. Chem. 2003, 278 (4), 2081-2084.
18. Mzhavia, N.; Pan, H.; Che, F. Y.; Fricker, L. D.; Devi, L. A. Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides. J. Biol. Chem. 2003, 278 (17), 14704-14711.
19. Malfroy, B.; Schwartz, J. C. Enkephalinase from rat kidney. Purification, characterization, and study of substrate specificity. J. Biol. Chem. 1984, 259 (23), 14365-14370.
20. Devault, A.; Nault, C.; Zollinger, M.; Fournie-Zaluski, M. C.; Roques, B. P.; Crine, P.; Boileau, G. Expression of neutral endopeptidase (enkephalinase) in heterologous COS-1 cells. Characterization of the recombinant enzyme and evidence for a glutamic acid residue at the active site. J. Biol. Chem. 1988a, 263 (8), 4033-4040.
21. Devault, A.; Sales, V.; Nault, C.; Beaumont, A.; Roques, B.; Crine, P.; Boileau, G. Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis. Histidine residues 583 and 587 are essential for catalysis. FEBS Lett. 1988b, 231 (1), 54-58.
22. Vijayaraghavan, J.; Kim, Y. A.; Jackson, D.; Orlowski, M.; Hersh, L. B. Use of site-directed mutagenesis to identify valine-573 in the S′1 binding site of rat neutral endopeptidase 24.11 (enkephalinase). Biochemistry 1990, 29 (35), 8052-8056.
23. Beaumont, A.; Le Moual, H.; Boileau, G.; Crine, P.; Roques, B. P. Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11). J. Biol. Chem. 1991, 266 (1), 214-220.
24. Kim, Y. A.; Shriver, B.; Quay, T.; Hersh, L. B. Analysis of the importance of arginine 102 in neutral endopeptidase (enkephalinase) catalysis. J. Biol. Chem. 1992, 267 (17), 12330-12335.
25. Dion, N.; Le Moual, H.; Crine, P.; Boileau, G. Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state. FEBS Lett. 1993, 318 (3), 301-304.
26. Dion, N.; Le Moual, H.; Fournie-Zaluski, M. C.; Roques, B. P.; Crine, P.; Boileau, G. Evidence that Asn542 of neprilysin (EC 3.4.24.11) is involved in binding of the P2′ residue of substrates and inhibitors. Biochem. J. 1995, 311 (Part 2), 623-627.
27. Sansom, C. E.; Hoang, V. M.; Turner, A. J. Molecular modeling of the active site of endothelin-converting enzyme. J Cardiovasc Pharmacol 1995, 26 (Suppl. 3), S75-S77.
28. Tiraboschi, G.; Jullian, N.; Thery, V.; Antonczak, S.; Fournie-Zaluski, M. C.; Roques, B. P. A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC.3.4.24.11). Protein Eng. 1999, 12 (2), 141-149.
29. Johnson, G. D.; Ahn, K. Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1. Anal. Biochem. 2000, 286 (1), 112-118.
30. Irwin, J. J.; Shoichet, B. K. ZINC - a free database of commercially available compounds for virtual screening. J. Chem. Inf. Model. 2005, 45 (1), 177-182.
31. Matthews, B. W. Structural bases of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 1988, 21 (9), 333-340.
32. Bur, D.; Dale, G. E.; Oefner, C. A three-dimensional model of endothelin-converting enzyme (ECE) based on the X-ray structure of neutral endopeptidase 24.11 (NEP). Protein Eng. 2001, 14 (5), 337-341.
33. Voisin, S.; Rognan, D.; Gros, C.; Ouimet, T. A three-dimensional model of the neprilysin 2 active site based on the X-ray structure of neprilysin. Identification of residues involved in substrate hydrolysis and inhibitor binding of neprilysin 2. J. Biol. Chem. 2004, 279 (44), 46172-46181.
34. Lee, S.; Debnath, A. K.; Redman, C. M. Active amino acids of the Kell blood group protein and model of the ectodomain based on the structure of neutral endopeptidase 24.11. Blood 2003, 102 (8), 3028-3034.
35. Ferro, C. J.; Webb, D. J. The clinical potential of endothelin receptor antagonists in cardiovascular medicine. Drugs 1996, 51 (1), 12-27.
36. Kohan, D. E. Endothelins in the normal and diseased kidney. Am. J. Kidney Dis. 1997, 29 (1), 2-26.
37. Humbert, M.; Simonneau, G. Drug insight: endothelin-receptor antagonists for pulmonary arterial hypertension in systemic rheumatic diseases. Nat. Clin. Pract. Rheumatol. 2005, 1 (2), 93-101.
38. Jeng, A. Y.; Mulder, P.; Kwan, A. L.; Battistini, B. Nonpeptidic endothelin-converting enzyme inhibitors and their potential therapeutic applications. Can. J. Physiol. Pharmacol. 2002, 80 (5), 440-449.
39. Ahn, K.; Sisneros, A. M.; Herman, S. B.; Pan, S. M.; Hupe, D.; Lee, C.; Nikam, S.; Cheng, X. M.; Doherty, A. M.; Schroeder, R. L.; Haleen, S. J.; Kaw, S.; Emoto, N.; Yanagisawa, M. Novel selective quinazoline inhibitors of endothelin converting enzyme-1. Biochem. Biophys. Res. Commun. 1998, 243 (1), 184-190.
40. Sansom, C. E.; Hoang, M. V.; Turner, A. J. Molecular modelling and site-directed mutagenesis of the active site of endothelin-converting enzyme. Protein Eng. 1998, 11 (12), 1235-1241.
41. Eswar, N.; Webb, B.; Marti-Renom, M. A.; Madhusudhan, M. S.; Eramian, D.; Shen, M. Y.; Pieper, U. ; Sali, A. Comparative protein structure modeling using modeller. Curr. Protoc. Bioinf. 2006, Chapter 5, Unit 5.6.
42. Sali, A.; Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234 (3), 779-815.
43. Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26, 283-291.
44. Morris, A. L.; MacArthur, M. W.; Hutchinson, E. G.; Thornton, J. M. Stereochemical quality of protein structure coordinates. Proteins 1992, 12 (4), 345-364.
45. Sipple, M. J. Recognition of errors in three-dimensional structures of proteins. Proteins: Struct., Funct., Bioinf. 1993, 17, 355-362.
46. Ginalski, K. Comparative modeling for protein structure prediction. Curr. Opin. Struct. Biol. 2006, 16 (2), 172-177.
47. Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 1998, 19 (14), 1639-1662.
48. Goodsell, D. S.; Morris, G. M.; Olson, A. J. Automated docking of flexible ligands: applications of AutoDock. J. Mol. Recognit. 1996, 9 (1), 1-5.
49. Solis, F. J.; Wets, R. J. Minimization by random search techniques. Math. Oper. Res. 1981, 6 (1), 19-30.