Differentiation of the local structure around tryptophan 51 and 64 in recombinant human erythropoietin by tryptophan phosphorescence

Photochemistry and Photobiology

Volumn 84, Issue 5, 2008, Pages 1172-1181

  Kerwin, Bruce A ^a   Aoki, Kenneth H ^a   Gonelli, Margherita ^b   Strambini, Giovanni B ^b  

^a AMGEN INC   (United States)

^b CNR Consiglio Nazionale delle Ricerche   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROPOIETIN; GLASS; RECOMBINANT PROTEIN; TRYPTOPHAN;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; HUMAN; LUMINESCENCE; MOLECULAR PROBE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SENSITIVITY AND SPECIFICITY; SPECTROFLUOROMETRY; TEMPERATURE; TIME; ULTRAVIOLET SPECTROPHOTOMETRY;

CIRCULAR DICHROISM; ERYTHROPOIETIN; GLASS; HUMANS; LUMINESCENCE; LUMINESCENT MEASUREMENTS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR PROBES; RECOMBINANT PROTEINS; SENSITIVITY AND SPECIFICITY; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; TIME FACTORS; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 50849126832     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2008.00307.x     Document Type: Article

References (61)

1. Vivian, J. T. P. R. Callis (2001) Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80, 2093 2109.
2. Galley, W. C. (1976) Concepts of Biochemical Fluorescence. Marcel Dekker, New York.
3. Hershberger, M. W., A. H. Maki W. C. Galley (1980) Phosphorescence and optically detected magnetic resonance studies of a class of anomalous tryptophan residues in globular proteins. Biochemistry 19, 2204 2209.
4. Strambini, G. B., P. Cioni R. A. Felicioli (1987) Characterization of tryptophan environments in glutamate dehydrogenases from temperature-dependent phosphorescence. Biochemistry 26, 4968 4975.
5. Strambini, G. B. E. Gabellieri (1989) Phosphorescence properties and protein structure surrounding tryptophan residues in yeast, pig, and rabbit glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 28, 160 166.
6. Gonnelli, M. G. B. Strambini (1995) Phosphorescence lifetime of tryptophan in proteins. Biochemistry 34, 13847 13857.
7. Gonnelli, M. G. B. Strambini (2005) Intramolecular quenching of tryptophan phosphorescence in short peptides and proteins. Photochem. Photobiol. 81, 614 622.
8. Saviotti, M. L. W. C. Galley (1974) Room temperature phosphorescence and the dynamic aspects of protein structure. Proc. Natl Acad. Sci. USA 71, 4154 4158.
9. Vanderkooi, J. M. (1992) Tryptophan phosphorescence from proteins at room temperature. In Topics in Fluorescence Spectroscopy: Volume 3: Biochemical Applications (Edited by J. R. Lakowicz pp. 113 136. Plenum Press, New York.
10. Cioni, P. G. B. Strambini (1998) Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold. J. Am. Chem. Soc. 120, 11749 11757.
11. Strambini, G. B. P. Cioni (1999) Pressure-temperature effects on oxygen quenching of protein phosphorescence. J. Am. Chem. Soc. 121, 8337 8344.
12. Strambini, G. B., E. Gabellieri, M. Gonnelli, S. Rahuel-Clermont G. Branlant (1998) Tyrosine quenching of tryptophan phosphorescence in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Biophys. J. 74, 3165 3172.
13. Strambini, G. B. E. Gabellieri (1991) Phosphorescence from Trp-48 in azurin - Influence of Cu(II), Cu(I), Ag(I) and Cd(II) at the coordination site. J. Phys. Chem. 95, 4352 4356.
14. Strambini, G. B. M. Gonnelli (1990) Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme. A comparative study of protein conformation in solution. Biochemistry 29, 196 203.
15. Cioni, P. G. B. Strambini (1989) Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectors. J. Mol. Biol. 207, 237 247.
16. Strambini, G. B., P. Cioni A. Puntoni (1989) Relationship between the conformation of glutamate dehydrogenase, the state of association of its subunit, and catalytic function. Biochemistry 28, 3808 3814.
17. Gabellieri, E. G. B. Strambini (2001) Structural perturbations of azurin deposited on solid matrices as revealed by trp phosphorescence. Biophys. J. 80, 2431 2438.
18. Strambini, G. B. M. Gonnelli (1986) Effects of urea and guanidine hydrochloride on the activity and dynamical structure of equine liver alcohol dehydrogenase. Biochemistry 25, 2471 2476.
19. Gonnelli, M. G. B. Strambini (1993) Glycerol effects on protein flexibility: A tryptophan phosphorescence study. Biophys. J. 65, 131 137.
20. Strambini, G. B. E. Gabellieri (1984) Intrinsic phosphorescence from proteins in the solid state. Photochem. Photobiol. 39, 725 729.
21. Strambini, G. B. E. Gabellieri (1996) Proteins in frozen solutions: Evidence of ice-induced partial unfolding. Biophys. J. 70, 971 976.
22. Cioni, P. G. B. Strambini (2002) Tryptophan phosphorescence and pressure effects on protein structure. Biochim. Biophys. Acta 1595 (1-2 116 130.
23. Imai, N., A. Kawamura, M. Higuchi, M. Oh-eda, T. Orita, T. Kawaguchi N. Ochi (1990) Physicochemical and biological comparison of recombinant human erythropoietin with human urinary erythropoietin. J. Biochem. 107, 352 359.
24. Takeuchi, M., S. Takasaki, H. Miyazaki, T. Kato, S. Hoshi, N. Kochibe A. Kobata (1988) Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. J. Biol. Chem. 263, 3657 3663.
25. Sasaki, H., B. Bothner, A. Dell M. Fukuda (1987) Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA. J. Biol. Chem. 262, 12059 12076.
26. Lai, P. H., R. Everett, F. F. Wang, T. Arakawa E. Goldwasser (1986) Structural characterization of human erythropoietin. J. Biol. Chem. 261, 3116 3121.
27. Israels, L. G. E. D. Israels (2003) Erythropoiesis: An overview. In Erythropoietins and Erythropoiesis (Edited by G. Molineux, M. A. Foote S. G. Elliott pp. 3 14. Birkhauser, Basel.
28. Jelkmann, W. E. Metzen (1996) Erythropoietin in the control of red cell production. Ann. Anat. 178, 391 403.
29. Markham, A. H. M. Bryson (1995) Epoetin alfa: A review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in nonrenal applications. Drugs 49, 232 254.
30. Lin, F. K., S. Suggs, C. H. Lin, J. K. Browne, R. Smalling, J. C. Egrie, K. K. Chen, G. M. Fox, F. Martin Z. Stabinsky (1985) Cloning and expression of the human erythropoietin gene. Proc. Natl Acad. Sci. USA 82, 7580 7584.
31. Jacobs, K., C. Shoemaker, R. Rudersdorf, S. D. Neill, R. J. Kaufman, A. Mufson, J. Seehra, S. S. Jones, R. Hewick E. F. Fritsch (1985) Isolation and characterization of genomic and cDNA clones of human erythropoietin. Nature 313, 806 810.
32. Cheetham, J. C., D. M. Smith, K. H. Aoki, J. L. Stevenson, T. J. Hoeffel, R. S. Syed, J. Egrie T. S. Harvey (1998) NMR structure of human erythropoietin and a comparison with its receptor bound conformation. Nat. Struct. Biol. 5, 861 866.
33. Deechongkit, S., K H. Aoki, S. S. Park B. A. Kerwin (2006) Biophysical comparability of the same protein from different manufacturers: A case study using Epoetin Alfa from Epogen and Eprex. J. Pharm. Sci. 95, 1931 1943.
34. Lah, J., I. Prislan, B. Krzan, M. Salobir, A. Francky G. Vesnaver (2005) Erythropoietin unfolding: Thermodynamics and its correlation with structural features. Biochemistry 44, 13883 13892.
35. Davis, J. M., T. Arakawa, T. W. Strickland D. A. Yphantis (1987) Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells. Biochemistry 26, 2633 2638.
36. Pace, C. N., F. Vajdos, L. Fee, G. Grimsley T. Gray (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411 2423.
37. Elliott, S., T. Lorenzini, D. Chang, J. Barzilay E. Delorme (1997) Mapping of the active site of recombinant human erythropoietin. Blood 89, 493 502.
38. Elliott, S., T. Lorenzini, S. Asher, K. Aoki, D. Brankow, L. Buck, L. Busse, D. Chang, J. Fuller, J. Grant, N. Hernday, M. Hokum, S. Hu, A. Knudten, N. Levin, R. Komorowski, F. Martin, R. Navarro, T. Osslund, G. Rogers, N. Rogers, G. Trail J. Egrie (2003) Enhancement of therapeutic protein in vivo activities through glycoengineering. Nat. Biotechnol. 21, 414 421.
39. Elliott, S., T. Lorenzini, D. Chang, J. Barzilay, E. Delorme, J. Giffin L. Hesterberg (1996) Fine-structure epitope mapping of antierythropoietin monoclonal antibodies reveals a model of recombinant human erythropoietin structure. Blood 87, 2702 2713.
40. Delorme, E., T. Lorenzini, J. Giffin, F. Martin, F. Jacobsen, T. Boone S. Elliott (1992) Role of glycosylation on the secretion and biological activity of erythropoietin. Biochemistry 31, 9871 9876.
41. Wigler, M., A. Pellicer, S. Silverstein R. Axel (1978) Biochemical transfer of single-copy eucaryotic genes using total cellular DNA as donor. Cell 14, 725 731.
42. Narhi, L. O., T. Arakawa, K. H. Aoki, R. Elmore, M. F. Rohde, T. Boone T. W. Strickland (1991) The effect of carbohydrate on the structure and stability of erythropoietin. J. Biol. Chem. 266, 23022 23026.
43. Venyaminov, S. Y. J. T. Yang (1996) Determination of protein secondary structure. In Circular Dichroism and the Conformational Analysis of Biomolecules (Edited by G. D. Fasman pp. 69 108. Plenum Press, New York/;London.
44. Strambini, G. B., B. A. Kerwin, B. D. Mason M. Gonnelli (2004) The triplet-state lifetime of indole derivatives in aqueous solution. Photochem. Photobiol. 80, 462 470.
45. Bodis, E., G. B. Strambini, M. Gonnelli, A. Malnasi-Csizmadia B. Somogyi (2004) Characterization of f-actin tryptophan phosphorescence in the presence and absence of tryptophan-free myosin motor domain. Biophys. J. 87, 1146 1154.
46. D'Auria, S., A. Varriale, M. Gonnelli, M. Saviano, M. Staiano, M. Rossi G. B. Strambini (2007) Tryptophan phosphorescence studies of the d-galactose/;d-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein. J. Proteome Res. 6, 1306 1312.
47. Greenfield, N. G. D. Fasman (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108 4116.
48. Veldhuis, G., E. Gabellieri, E. P. P. Vos, B. Poolman, G. B. Strambini J. Broos (2005) Substrate-induced conformational changes in the membrane-embedded IIC(mtl)-domain of the mannitol permease from Escherichia coli, EnzymeII(mtl), probed by tryptophan phosphorescence spectroscopy. J. Biol. Chem. 280, 35148 35156.
49. Strambini, G. B. M. Gonelli (1995) Tryptophan phosphorescence in fluid solution. J. Am. Chem. Soc. 117, 7646 7651.
50. Kerwin, B. A., B. S. Chang, C. V. Gegg, M. Gonnelli, T. Li G. B. Strambini (2002) Interactions between PEG and type I soluble tumor necrosis factor receptor: Modulation by pH and by PEGylation at the N terminus. Protein Sci. 11, 1825 1833.
51. Cioni, P., J. J. Onuffer G. B. Strambini (1992) Characterization of tryptophan phosphorescence of aspartate aminotransferase from Escherichia coli. Eur. J. Biochem. 209, 759 764.
52. Schlyer, B. D., E. Lau A. H. Maki (1992) A comparative investigation of snake venom neurotoxins and their triplet-state tryptophan-disulfide interactions using phosphorescence and optically detected magnetic resonance. Biochemistry 31, 4375 4383.
53. Li, Z., A. Bruce W. C. Galley (1992) Temperature dependence of the disulfide perturbation to the triplet state of tryptophan. Biophys. J. 61, 1364 1371.
54. Li, Z., W. E. Lee W. C. Galley (1989) Distance dependence of the tryptophan-disulfide interaction at the triplet level from pulsed phosphorescence studies on a model system. Biophys. J. 56, 361 367.
55. Dedonder-Lardeux, C., C. Jouvet, S. Perun A. L. Sobolewski (2003) External electric field effect on the lowest excited states of indole: Ab initio and molecular dynamics study. Phys. Chem. Chem. Phys. 5, 5118 5126.
56. Hahn, D. K. P. R. Callis (1997) Lowest triplet state of indole - An ab initio study. J. Phys. Chem. 101, 2686 2691.
57. Hershberger, M. V., A. H. Maki W. C. Galley (1980) Phosphorescence and optically detected magnetic resonance studies of a class of anomalous tryptophan residues in globular proteins. Biochemistry 19, 2204 2209.
58. Martinez-Oyanedel, J., H. W. Choe, U. Heinemann W. Saenger (1991) Ribonuclease T1 with free recognition and catalytic site: Crystal structure analysis at 1.5 A resolution. J. Mol. Biol. 222, 335 352.
59. Fraczkiewicz, R. W. Braun (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19, 319 333.
60. Banks, D. D. B. A. Kerwin (2004) A deoxygenation system for measuring protein phosphorescence. Anal. Biochem. 324, 106 114.
61. Cioni, P., E. Gabellieri, M. Gonnelli G. B. Strambini (1994) Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosphorescence. Biophys. Chem. 52, 25 34.