Structural characterization of bovine granulocyte colony stimulating factor: Effect of temperature and pH

Journal of Pharmaceutical Sciences

Volumn 92, Issue 9, 2003, Pages 1793-1804

  Kueltzo, Lisa A ^a,b   Middaugh, C Russell ^a  

^a UNIVERSITY OF KANSAS   (United States)

^b UNIVERSITY OF COLORADO   (United States)

Author keywords

Absorption spectroscopy; Biophysical models; Calorimetry (DSC); Circular dichroism; Fluorescence spectroscopy; Infrared spectroscopy; Protein aggregation; Protein formulation; Protein structure; UV Vis spectroscopy

Indexed keywords

CYTOKINE; GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR;

ARTICLE; CATTLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; DRUG FORMULATION; FLUORESCENCE; INFRARED SPECTROSCOPY; OPTICAL DENSITY; PH; PROTEIN CONFORMATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

EID: 0041336629     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1002/jps.10440     Document Type: Article

References (25)

1. Grillo AO, Edwards KL, Kashi RS, Shipley KM, Hu L, Besman MJ, Middaugh CR. 2001. Conformational origin of the aggregation of recombinant human factor VIII. Biochemistry 40:586-595.
2. Kueltzo LA, Normand N, O'Hare P, Middaugh CR. 2000. Conformational lability of herpes virus protein VP22. J Biol Chem 275:33213-33221.
3. Choosakoonkriang S, Wiethoff CM, Anchordoquy TJ, Koe GS, Smith JG, Middaugh CR. 2001. Infrared spectroscopic characterization of the interaction of cationic lipids with plasmid DNA. J Biol Chem 276:8037-8043.
4. Lobo BA, Davis A, Koe G, Smith JG, Middaugh CR. 2001. Isothermal titration calorimetric analysis of the interaction between cationic lipids and plasmid DNA. Arch Biochem Biophys 386:95-105.
5. Lobo BA, Rogers SA, Choosakoonkriang S, Smith JG, Koe G, Middaugh CR. 2002. Differential scanning calorimetric studies of the thermal stability of plasmid DNA complexed with cationic lipids and polymers. J Pharm Sci 91:454-466.
6. Wiethoff CM, Gill ML, Koe GS, Koe JG, Middaugh CR. 2002. The structural organization of cationic lipid-DNA complexes. J Biol Chem 277:44980-44987.
7. Hubel K, Dale DC, Liles WC. 2002. Therapeutic use of cytokines to modulate phagocyte function for the treatment of infectious diseases: Current status of granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, macrophage colony-stimulating factor, and interferon-gamma. J Infect Dis 185:1490-1501.
8. Kasraian K, Kuzniar A, Earley D, Kamicker BJ, Wilson G, Manion T, Hong J, Reiber C, Canning P. 2001. Sustained in vivo activity of recombinant bovine granulocyte colony stimulating factor (rbG-CSF) using HEPES buffer. Pharm Dev Technol 6:441-447.
9. Lovejoy B, Cascio D, Eisenberg D. 1993. Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF). J Mol Biol 234:640-653.
10. Provencher S, Glockner J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33-37.
11. Sreerama N, Woody R. 1990. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209: 32-44.
12. Manavalan P, Johnson WC Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal Biochem 167:76-85.
13. Sreerama N. CDPro: A software package for analyzing protein spectra. Access at: http://lamar.colostate.edu/~sreeram/CDPro/index.html.
14. De Filippis V, de Laureto PP, Toniutti N, Fontana A. 1996. Acid-induced molten globule state of a fully active mutant of human interleukin-6. Biochemistry 35:11503-11511.
15. Schein CH. 2002. The shape of the messenger: using protein structure information to design novel cytokine-based therapeutics. Curr Pharm Des 8: 2113-2129.
16. Bartkowski R, Kitchel R, Peckham N, Margulis L. 2002. Aggregation of recombinant bovine granulocyte colony stimulating factor in solution. J Protein Chem 21:137-143.
17. Arai M, Kuwajima K. 2000. Role of the molten globule state in protein folding. Adv Protein Chem 53:209-282.
18. Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
19. Narhi LO, Kenney WC, Arakawa T. 1991. Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride. J Protein Chem 10: 359-367.
20. Kolvenbach CG, Elliott S, Sachdev R, Arakawa T, Narhi LO. 1993. Characterization of two fluorescent tryptophans in recombinant human granulocyte-colony stimulating factor: Comparison of native sequence protein and tryptophan-deficient mutants. J Protein Chem 12:229-236.
21. Krishnan S, Chi EY, Webb JN, Chang BS, Shan D, Goldenberg M, Manning MC, Randolph TW, Carpenter JF. 2002. Aggregation of granulocyte colony stimulating factor under physiological conditions: characterization and thermodynamic inhibition. Biochemistry 41:6422-6431.
22. Chi EY, Krishnan S, Kendrick BS, Chang BS, Carpenter JF, Randolph TW. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 12:903-913.
23. Redfield C, Smith RA, Dobson CM. 1994. Structural characterization of a highly-ordered 'molten globule' at low pH. Nat Struct Biol 1:23-29.
24. Kolvenbach CG, Narhi LO, Philo JS, Li T, Zhang M, Arakawa T. 1997. Granulocyte-colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH 2. J Pept Res 50: 310-318.
25. Dryden D, Weir MP. 1991. Evidence for an acid-induced molten-globule state in interleukin-2: A fluorescence and circular dichroism study. Biochim Biophys Acta 1078:94-100.