Degradation of Myoglobin by Polymeric Artificial Metalloproteases Containing Catalytic Modules with Various Catalytic Group Densities: Site Selectivity in Peptide Bond Cleavage

Journal of the American Chemical Society

Volumn 125, Issue 47, 2003, Pages 14580-14589

  Yoo, Chang Eun ^a   Chae, Pil Seok ^a   Kim, Jung Eun ^a   Jeong, Eui June ^a   Suh, Junghun ^a  

^a Seoul National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

DINUCLEAR CATALYSTS;

CHEMICAL BONDS; CRYSTAL STRUCTURE; DEGRADATION; ENZYMES; HYDROLYSIS; X RAY CRYSTALLOGRAPHY;

CATALYST SELECTIVITY;

CARBOXYLIC ACID DERIVATIVE; COPPER COMPLEX; ENZYME; HEME DERIVATIVE; METALLOPROTEINASE; MYOGLOBIN; POLYMER; POLYSTYRENE;

ARTICLE; CATALYSIS; CATALYST; CHEMICAL BOND; COMPLEX FORMATION; HYDROLYSIS; MOLECULAR MODEL; PROTEIN DEGRADATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; BIOMIMETIC MATERIALS; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COPPER; HORSES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; METALLOPROTEASES; MODELS, MOLECULAR; MYOGLOBIN; ORGANOMETALLIC COMPOUNDS; PROTEIN CONFORMATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0344443325     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja034730t     Document Type: Article

References (65)

1. Klotz, I. M. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry; London, 1987; Chapter 2.
2. Wulff, G. Angew. Chem., Intl. Ed. Engl. 1995, 34, 1812-1832.
3. Suh, J. In Polvmeric Materials Encyclopedia; Salamone, J. C., Ed.; CRC Press: Boca Raton, 1996; 4210-4218 and 8230-8237.
4. Hodge, P. Chem. Soc. Rev. 1997, 26, 417-424.
5. Suh, J. Adv. Supramolecular Chem. 2000, 6, 245-286.
6. Suh, J. Synlett. 2001, 9, 1343-1363.
7. Suh, J. Acc. Chem. Res. 2003, 36, 562-570.
8. Dugas, H. Bioorganic Chemistry, 3rd ed.; Springer-Verlag: New York, 1996; p3, 172, and 255.
9. Silverman, R. B. In The Organic Chemistry of Drug Design and Drug Action; Academic Press: San Diego, 1992; pp 103-113.
10. Sutton, P. A.; Buckingham, D. A. Acc. Chem. Res. 1987, 20, 357-364.
11. Chin, J. Acc. Chem. Res. 1991, 24, 145-152.
12. Suh, J. Acc. Chem. Res. 1992, 25, 273-279.
13. Suh, J. In Perspectives on Bioinorganic Chemistry; Hay, R. W., Dilworth, J. R., Nolan, K. B., Eds.: JAI Press: London, 1996; Vol. 3, 115-149.
14. Chin, J.; Jubian, V.; Mrejen, K. J. Chem. Soc., Chem. Commun. 1990 1326-1328.
15. Rana, T. M.; Meares, C. F. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 10 578-10 582.
16. Zhu, L.; Qin, L.; Parac, T. N.; Kostic, N. M. J. Am. Chem. Soc. 1994, 116 5218-5224.
17. Hegg, E. L.; Burstyn, J. N J. Am. Chem. Soc. 1995, 117, 7015-7016.
18. Kaminskaia, N. V.; Johnson, T. W.; Kostic, N. M. J. Am. Chem. Soc. 1999 121, 8663-8664.
19. Saha, M. K.; Bernal, I. J. Chem. Soc., Chem. Commun. 2003, 612-613
20. Suh, J.; Park, T. H.; Hwang, B. K. J. Am. Chem. Soc. 1992, 114. 5141-5146.
21. Suh, J.; Cho, Y.; Lee, K. J. J. Am. Chem. Soc. 1991, 113, 4198-4202.
22. Jang, B.-B.; Lee, K. P.; Min, D. H.; Suh, J. J. Am. Chem. Soc. 1998, 126 12 008-12 016.
23. Suh, J.; Hong, S. H. J. Am. Chem. Soc. 1998, 120, 12 545-12 552.
24. Moon, S.-J.; Jeon, J. W.; Kim, H.; Suh, M. P.; Suh, J. J. Am. Chem. Soc 2000, 122, 7742-7749.
25. Suh, J.; Moon, S.-J. Inorg. Chem. 2001, 40, 4890-4895.
26. Jeung, C. S.; Kim, C. H.; Min, K.; Suh, S. W.; Suh, J. Bioorg. Med. Chem. Lett. 2001, 11, 2401-2404.
27. Jeung, C.-S.; Song, J. B.; Kim, Y.-H.; Suh, J. Bioorg. Med. Chem. Lett. 2001, 11. 3061-3064.
28. Jeon, J.; Son, S. J.; Yoo, C. E.; Hong, I. S.; Song, J. B.; Suh, J. Org. Let 2002, 4, 4155-4158.
29. Suh, J.; Lee, S. H.; Zoh, K. D. J. Am. Chem. Soc. 1992, 114, 7916.
30. Suh, J.; Hah, S. S. J. Am. Chem. Soc. 1998, 120, 10 088-10 093.
31. Suh, J.; Oh, S. J. Org. Chem. 2000, 65, 7534-7540.
32. Oh, S.; Chang, W.; Suh. J. Bioorg. Med. Chem. Lett. 2001, 11, 1469-1472.
33. Kim, H.; Paik, H.; Kim, M.-s.; Chung, Y.-S.; Suh, J. Bioorg. Med. Chem. Lett. 2002, 12, 2557-2560.
34. Kim, H.; Kim, M.-s.; Paik, H.; Chung, Y.-S.; Hong, I. S.; Suh, J. Bioorg. Med. Chem. Lett. 2002, 12, 3247-3250.
35. Tahirov, T. H.; Oki, H.; Tsukihara, T.; Ogasahara, K.; Yutani, K.; Ogata, K.; Izu, Y.; Tsunasawa, S.; Kato, K. J. Mol. Biol. 1998, 284, 101-124.
36. Paul-Soto, R.; Bauer, R.; Frére, J.-M.; Galleni, M.; Meyer-Klaucke, W.; Nolting, H.; Rossolini, G. M.; de Seny, D.; Hernandez-Valladares, M.; Zeppezauer, M.; Adolph, H.-W. J. Biol. Chem. 1999, 274, 13 242-13 249.
37. Mock, W. L.; Liu, Y. J. Biol. Chem. 1995, 270, 18 437-18 446.
38. Lippard, S. J. Science 1995, 268, 996-997.
39. Carvajal, N.; López, V.; Salas, M.; Uribe, E.; Herrera, P.; Cerpa, J. Biochem. Biophys. Res. Comm. 1999, 258, 808-811.
40. Williams, N. H.; Takasaki, B.; Wall, M.; Chin, J. Acc. Chem. Res. 1999, 32. 485-493.
41. Finn, G.; Sharpless, K. B. J. Am. Chem. Soc. 1991, 113, 113-126.
42. Shibasaki, M.; Sasai, J.; Arai, T. Angew. Chem., Int. Ed. Engl. 1997, 36, 1236-1256.
43. Corey, E. J.; Bakshi, R. K.; Shibata, S. J. Am. Chem. Soc. 1987, 109, 5551-5553.
44. Izatt, R. M.; Pawlak, K.; Bradshaw, J. S. Chem. Rev. 1991, 91, 1721-2085.
45. Merrifield, B. In Nobel Lectures in Chemistry (1981-1990); Frängsmyr, T. Ed.; World Scientific: Singapore, 1992; pp 143-175.
46. Bodwell, C. E.; McClain P. E. In The Science of Meat and Meat Products, 2nd ed.; Price, J. F.; Schweigert, B. S. Ed.; W. H. Freeman: San Francisco, 1971; p 97.
47. Lameli, U. K. Nature 1970, 227, 680-685.
48. Hames, B. D. In Gel Electrophoresis of Proteins; Hames, B. D., Rickwood, D., Eds.; IRL Press: New York, 1990; Chapter 1.
49. The quality of data points in Figures 4 and 5 is not high. This has been also observed in kinetic studies with other polymeric artificial proteases.25-27.33 The erratic data points may be ascribed to several sources: accurate measurement of densities of the parent electrophoretic band is sometimes difficult, the parent electrophoretic band may contain large degradation products in addition to the uncleaved protein substrate, properties of surface of the polymeric catalyst may be affected by pH changes which is not easily predicted, and so on. Despite scattered data points in Figures 4 and 5, the general shape of the pH profile and the optimum pH may be accurately identified and the value of a kinetic parameter measured at the optimum pH can be taken as the representative value of the catalyst.
50. Gly is the C-terminal residue of the protein fragments with m/z of 6578 and 6868 whereas Ala is that of 10 382. The low reactivity of these protein fragments toward CPA is consistent with the substrate selectivity51 of CPA.
51. Zeffren, E.; Hall. P. L. The Study of Enzyme Mechanism; Wiley: New York, 1973; pp 73, 79-86, 196.
52. Evans, S. V.; Brayer, G. D. J. Mol. Biol. 1990, 213, 885-897.
53. Negligible hydrolysis of the peptide bonds of the catalytic modules either on the surface of PS or in the bulk water suggests that the intramolecular attack by the Cu(II)Cyc group at the peptide linkage involves steric strain.
54. Stryer, L., Freeman, W. H., Eds.; Biochemistry; New York, 1995; 4th, p 149.
55. Bryant, R. A. R.; Hansen, D. A. J. Am. Chem. Soc. 1996, 118. 5498-5499.
56. Radzicka, A.; Wolfenden, R. J. Am. Chem. Soc. 1996, 118, 6105-6109.
57. Gao, C.; Lavey, B. J.; Lo, C.-H. L.; Datta, A.; Wentworth, P., Jr.; Janda, K. D. J. Am. Chem. Soc. 1998, 120, 2211-2217.
58. Histidyl imidazole is utilized as a ligand for Cu(II) ion in various Cu(II) enzymes such as ascorbate oxidase, plastocycanin, hemocyanin, and copper zinc superoxide dismutase.59
59. Lippard, S. J.; Berg, J. M. Principles of Bioinorganic Chemistry; University Science Books: Mill Valley, 1994; pp 87, 241, 285, 286, 300, 328.
60. MS/Ac.51
61. -4 M) revealed, however, neither the oligopeptide nor its hydrolysis products containing the cinnamoyl chromophore were detected. This indicates ready adsorption of the oligopeptide substrate and/or its hydrolysis products onto the resins.
62. For example, another derivative of polystyrene containing Cu(II)Cyc prepared in a previous study effectively cleaved22 γ-globulin. This catalyst, however, was not effective toward albumin. On the other hand. an artificial protease prepared by construction of an artificial active site comprising three salicylate residues on polystyrene effectively cleaved albumin32 but was not active toward γ-globulin. Similarly, an artificial protease prepared by attaching two or more proximal imidazoles on polystyrene manifested high proteolytic activity toward albumin31 but did not cleave γ-globulin.
63. If the protein substrates or their hydrolysis products are bound too strongly and, thus, adsorbed onto the polymeric support, then the polymer has little catalytic value. For example, γ-globulin and albumin are strongly adsorbed onto the Amberlite weakly acidic cation exchanger in which polystyrene is the matrix and carboxyl group is the active group.64
64. Kim, H.; Chung, Y.-S.; Paik, H.; Kim, M.-s.; Suh, J. Bioorg. Med. Chem. Lett. 2002, 12, 2663-2666.
65. Sarin, V. K.; Kent, S. B. H.; Tam, J. P.; Merrifield, R. B. Anal. Biochem. 1981, 117, 147-157.