Synthesis and NMR structure of P41icf, a potent inhibitor of human cathepsin L

Journal of the American Chemical Society

Volumn 125, Issue 6, 2003, Pages 1508-1517

  Chiva, Cristina ^b   Barthe, Philippe ^b   Codina, Anna ^b   Gairf, Margarida ^b   Molina, Franck ^c   Granier, Claude ^c   Pugnière, Martine ^c   Inui, Tatsuya ^d   Nishio, Hideki ^d   Nishiuchi, Yuji ^d   Kimura, Terutoshi ^d   Sakakibara, Shumpei ^d   Albericio, Fernando ^a,b   Giralt, Ernest ^a,b  

^a INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^b UNIVERSITY OF BARCELONA   (Spain)

^c CNRS   (France)

^d Peptide Institute Inc   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; BIOCHEMISTRY; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SURFACE PLASMON RESONANCE;

DENATURATION;

PROTEINS;

CATHEPSIN L; DISULFIDE; IMMUNOGLOBULIN FRAGMENT; PEPTIDE DERIVATIVE; PROTEIN DERIVATIVE; PROTEIN P41ICF; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; HUMAN; NUCLEAR MAGNETIC RESONANCE; OXIDATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SYNTHESIS; SURFACE PLASMON RESONANCE; SYNTHESIS;

AMINO ACID SEQUENCE; ANTIGENS, DIFFERENTIATION, B-LYMPHOCYTE; CATHEPSINS; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; HISTOCOMPATIBILITY ANTIGENS CLASS II; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SOLUTIONS; SURFACE PLASMON RESONANCE;

EID: 0346036170     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0207908     Document Type: Article

References (46)

1. Bevec, T.; Stoka, V.; Pungercic, G.; Dolenc, I.; Turk, V. J. Exp. Med. 1996, 183, 1331.
2. Molina, F.; Pau, B.; Granier, C. FEBS Lett. 1996, 391, 229.
3. Molina, F.; Bouanani, M.; Pau, B.; Granier, C. Eur. J. Biochem 1996, 240, 125.
4. Peterson, M.; Miller, J. Nature 1992, 357, 596.
5. Cresswell, P. Cell 1996, 84, 505.
6. Gunear, G.; Pungercic, G.; Klemencic, I.; Turk, V.; Turk, D. EMBO J. 1999, 18, 793.
7. Millest, A. J.; Breen, S. A.; Loveday, B. E.; Clarkson, P. N.; Simpson, C. A.; Waterton, J. C.; Johnstone, D. Bone 1997, 20, 465.
8. Esser, R. E.; Angelo, R. A.; Murphey, M. D.; Watts, L. M.; Thomburg, L. P.; Palmer, J. T.; Talhouk, J.; Smith, R. E. Arthritis Rheum. 1994, 37, 236.
9. Yagel, S.; Warner, A. H.; Nellans, H. N.; Lala, P. K.; Waghome, C.; Denhardt, D. T. Cancer Res. 1989, 49, 3553.
10. Brinker, A.; Weber, E.; Stoll, D.; Voigt, J.; Müller, A.; Sewald, N.; Jung, G.; Wiesmüller, K. H.; Bohley, P. Eur. J. Biochem. 2000, 267, 5085.
11. McGrath, M. E. Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 181.
12. Turk, B.; Turk, D.; Turk, V. Biochim. Biophys. Acta 2000. 1477, 98.
13. Chiva, C. PhD Thesis, University of Barcelona, Barcelona, Spain, 2001.
14. Lloyd-Williams, P.; Albericio, F.; Giralt, E. Chemical Approaches to the Synthesis of Peptides and Proteins. CRC Press: Boca Raton, 1997.
15. Nishiuchi, Y.; Inui, T.; Nishio, H.; Bódi, J.; Kimura, T.; Tsuji, F. I.; Sakakibara, S. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 13549.
16. (a) Barlos, K.; Gatos, D.; Kallitsis, J.; Papaphotiu, G.; Sotiriu, P.; Wenqing, Y.; Schäfer, W. Tetrahedron Lett. 1989, 30. 3943.
17. (b) Barlos, K.; Gatos, D.; Kapolos, S.; Papaphotiu, G.; Schäfer, W.; Wenqing, Y. Tetrahedron Lett. 1989, 30, 3947.
18. (c) Barlos, K.; Chatzi, O.; Gatos, D.; Stavropoulos, G. Int. J. Pept. Protein Res. 1991, 37, 513.
19. Chiva, C.; Vilaseca, M.; Giralt, E.; Albericio, F. J. Pept. Sci. 1999, 5, 131.
20. Nishiuchi, Y.; Nishio, H.; Inui, T.; Bódi, J.; Kimura, T. J. Pept. Sci. 2000, 6, 84.
21. (a) Rabanal, F.; Giralt, E.; Albericio, F. Tetrahedron Lett. 1992, 33, 1775.
22. (b) Rabanal, F.; Giralt, E.; Albericio, F. Tetrahedron 1995, 51, 1449.
23. Bódi, J.; Nishiuchi, Y.; Nishio, H.; Inui, T.; Kimura, T. Tetrahedron Lett. 1998, 39, 7117.
24. Nishiuchi, Y.; Nishio, H.; Inui, T.; Kimura, T.; Sakakibara, S. Tetrahedron Lett. 1996, 37, 7529.
25. Kumagaye, K. Y.; Inui, T.; Nakajima, K.; Kimura, T.; Sakakibara, S. Pept. Res. 1991, 4, 84.
26. Nishio, H.; Kimura, T.; Sakakibara, S. Tetrahedron Lett. 1994, 35, 1239.
27. Woody, R. W. Biopolymers 1978, 17, 1451.
28. Woody R. W. In Circular dichroism. Principles and Applications; Nakanishi, K., Berova, N., Woody, R. W., Eds.; VCH Publishers Inc.: New York, USA, 1994; p 473.
29. Wüthrich, K, NMR of proteins and nucleic acids; Wiley and Sons: New York, 1986.
30. Wishart, D. S.; Bigam, C. G.; Holm, A.; Hodges, R. S.; Sykes, B. D. J. Biomol. NMR 1995, 5, 67.
31. Pearlman, D. A.; Case, D. A.; Caldwell, J. W.; Ross, W. S.; Cheatham, T. E., III; DeBolt, S.; Ferguson, D.; Seibel, G.; Kollman, P. Comput. Phys. Commun. 1995, 91, 1.
32. Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thomton, J. M. J. Appl. Crystallogr. 1993, 26, 283.
33. Srinivasan, N.; Sowdhamini, R.; Ramakrishnan, C.; Balaram, P. Int. J. Pept. Protein Res. 1990, 36, 147.
34. Johnson, T.; Quibell, M.; Sheppard, R. C. J. Pept. Sci. 1995, 1, 11.
35. Wöhr, T.; Wahl, F.; Nefzi, A.; Rohwedder, B.; Sato, T.; Sun, X.; Mutter, M. J. Am. Chem. Soc. 1996, 118, 9218.
36. Dawson, P. Synthesis of Peptides and Peptidomimetics; Goodman. M., Felix, A., Moroder, L., Toniolo, C., Eds.; Houben-Weyl. Methods of Organic Chemistry, Vol. E22a; Thieme: Stuttgart, Germany and New York, 2002; pp 627-641.
37. Okada, Y. Synthesis of Peptides and Peptidomimetics: Goodman, M., Felix, A., Moroder, L., Toniolo, C., Eds.; Houben-Weyl. Methods of Organic Chemistry, Vol. E22a; Thieme: Stuttgart, Germany and New York, 2002; pp 591-626.
38. Wetlaufer, D. B.; Xie, Y. Protein Sci. 1995, 4, 1535.
39. Cathepsin L activity is very pH sensitive (Mason, R. W.; Green, G. G.; Barrett, A. J. Biochem. J. 1985, 226, 233-241.). Bevec and co-workers, in their experiment, performed the assay under more basic conditions than we did. Under these conditions, the cathepsin could be less active and, as they followed the inactivation of the functional activity of cathepsin L using a subtract (and not the direct binding of the two molecules), a loss in the optimal activity of the enzyme should result in a greater dissociation constant.
40. Schnölzer Schnblzer, M.; Alewood, P.; Jones, A.; Alewood, D.; Kent, S. B. H. Int. J. Pept. Protein Res. 1992, 40, 180.
41. Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. J. Biomol. NMR 1995, 6, 277.
42. Johnson, B. A.; Blevins, R. A. J. Biomol. NMR 1994, 4, 603.
43. Ludvingsen, S.; Andersen, K. V.; Poulsen, F. M. J. Mol. Biol. 1991, 217, 731.
44. Hyberts, S. G.; Märki, W.; Wagner, G. Eur. J. Biochem. 1987, 164, 625.
45. Gümert, P.; Mumenthaler, C.; Wüthrich, K. J. Mol. BioL Biol. 1997, 273, 283.
46. Case, D. A.; Pearlman, D. A.; Caldwell, J. W.; Cheatham, T. E., III; Ross, W. S.; Sirmerling, C. L.; Darden, T. A.; Merz, K. M.; Stanton R. V.; Cheng, A. L.; Vincent, J. J.; Crowley, M.; Ferguson, D. M.; Radner, R. J.; Seibel, G. L.; Singh, U. C.; Weiner, P. K.; Kollman, P. A. AMBER 5; University of California, San Francisco, 1997.