Thermal stability: A means to assure tertiary structure in therapeutic proteins

Biologicals

Volumn 30, Issue 3, 2002, Pages 175-185

  Cauchy, Mike ^a   D'Aoust, Sophie ^a   Dawson, Brian ^a   Rode, Harold ^a   Hefford, Mary Alice ^a  

^a HEALTH CANADA   (Canada)

Author keywords

FTIR; Protein structure; Quality assurance; Stability; Therapeutic proteins; Thermal denaturation

Indexed keywords

RECOMBINANT GROWTH HORMONE;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; HYDROGEN BOND; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; THERMOSTABILITY;

EID: 0036771287     PISSN: 10451056     EISSN: None     Source Type: Journal    
DOI: 10.1006/biol.2002.0322     Document Type: Article

References (33)

1. Ultsch M.H., Somers W., Kossiakoff A.A., De Vos A.M. The crystal structure of affinity-matured human growth hormone at 2 A resolution. J Mol Biol. 236:1994;286-299.
2. Wells J.A., De Vos A.M. Structure and function of human growth hormone: implications for the hematopoietins. Annu Rev Biophys Biomol Struct. 22:1993;329-351.
3. Abildgaard F., Jorgensen A.M., Led J.J., Christensen T., Jensen E.B., Junker F., Dalboge H. Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone. Biochemistry. 31:1992;8587-8596.
4. Aloj S., Edelhoch H. The molecular properties of human growth hormone. J Biol Chem. 247:1972;1146-1152.
5. Piotto M., Saudek V., Sklenar V. J Biomolec Nucl Med Res. 2:1992;661-666.
6. Sklenar V., Piotto M., Leppik R., Saudek V. J Magn Reson Ser A. 102:1993;241-245.
7. Costantino H.R., Carrasquillo K.G., Cordero R.A., Mumenthaler M., Hsu C.C., Griebenow K. Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone. J Pharm Sci. 87:1998;1412-1420.
8. Pace C.N. The stability of globular proteins. Creighton T. Protein Structure, A Practical Approach. 1975;1-43 IRL Press, New York.
9. Mantsch H.H., Casal H.L., Jones R.N. Resolution enhancement of infrared spectra of biological systems. Clark R.J.H., Hester R.E. Spectroscopy of Biological Systems. 1986;1-46 John Wiley and Sons, New York.
10. Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 25:1986;469-487.
11. Turner C., Cary P.D., Grego B., Hearn M.T., Chapman G.E. A proton-nuclear-magnetic-resonance study of human somatotropin (growth hormone). Assignment and properties of the histidine residues. Biochem J. 213:1993;107-113.
12. DeFelippis M.R., Kilcomons M.A., Lents M.P., Youngman K.M., Havel H.A. Acid stabilization of human growth hormone equilibrium folding intermediates. Biochem Biophys Acta. 1247:1995;35-45.
13. Costantino H.R., Schwendeman S.P., Griebenow K., Klibanov A.M., Langer R. The secondary structure and aggregation of lyophilized tetanus toxoid. J Pharm Sci. 85:1996;1290-1293.
14. Dong A., Prestrelski S.J., Allison S.D., Carpenter J.F. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J Pharm Sci. 84:1995;415-424.
15. Görne-Tschelnokow U., Naumann D., Weise C., Hucho F. Secondary structure and temperature behaviour of acetylcholinesterase. Studies by Fourier-transform infrared spectroscopy. Eur J Biochem. 213:1993;1235-1242.
16. Zhao F., Ghezzo-Schneich E., Aced G.I., Hong J., Milby T., Schneich C. Metal-catalyzed oxidation of histidine in human growth hormone. Mechanism, isotope effects, and inhibition of a mild denaturing alcohol. J Biol Chem. 272:1997;9019-9029.
17. Casal H.L., Köhler U., Mantsch H.H. Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochim Biophys Acta. 957:1988;11-20.
18. Surewicz W.K., Olesen P.R. On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy. Biochemistry. 34:1995;9655-9660.
19. Yang Y.H., Dong A., Meyer J., Johnson O.L., Cleland J.L., Carpenter J.F. Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres. J Pharm Sci. 88:1999;161-165.
20. Carrasquillo K.G., Costantino H.R., Cordero R.A., Hsu C.C., Griebenow K. On the structural preservation of recombinant human growth hormone in a dried film of a synthetic biodegradable polymer. J Pharm Sci. 88:1999;166-173.
21. Costantino H.R., Nguyen T.H., Hsu C.C. Fourier-transform Infrared Spectroscopy demonstrates that lyophilization alters the secondary structure of recombinant human growth hormone. Pharmaceutical Sciences. 2:1996;229-232.
22. Costantino H.R., Carrasquillo K.G., Cordero R.A., Mumenthaler M., Hsu C.C., Griebenow K. Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone. J Pharm Sci. 87:1998;1412-1420.
23. Yang T.H., Dong A., Meyer J., Johnson O.L., Cleland J.L., Carpenter J.F. Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres. J Pharm Sci. 88:1999;161-165.
24. Sundstrom M., Lundqvist T., Rodin J., Giebel L.B., Milligan D., Norstedt G. Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2·9 A resolution. J Biol Chem. 271:1996;32197-32203.
25. Ultsch M., De Vos A.M. Crystals of human growth hormone-receptor complexes. Extracellular domains of the growth hormone and prolactin receptors and a hormone mutant designed to prevent receptor dimerization. J Mol Biol. 231:1993;1133-1136.
26. Ultsch M.H., Somers W., Kossiakoff A.A., De Vos A.M. The crystal structure of affinity-matured human growth hormone at 2 A resolution. J Mol Biol. 236:1994;286-299.
27. Aloj S., Edelhoch H. The molecular properties of human growth hormone. J Biol Chem. 247:1972;1146-1152.
28. Brems D.N., Brown P.L., Becker G.W. Equilibrium denaturation of human growth hormone and its cysteine-modified forms. J Biol Chem. 265:1990;5504-5511.
29. Polverino D.L., Toma S., Tonon G., Fontana A. Probing the structure of human growth hormone by limited proteolysis. Int J Pept Protein Res. 45:1995;200-208.
30. Wicar S., Mulkerrin M.G., Bathory G., Khundkar L.H., Karger B.L. Conformational changes in the reversed phase liquid chromatography of recombinant human growth hormone as a function of organic solvent: the molten globule state. Anal Chem. 66:1994;3908-3915.
31. Kasimova M.R., Milstein S.J., Freire E. The conformational equilibrium of human growth hormone. J Mol Biol. 277:1998;409-418.
32. Dong A., Randolph T.W., Carpenter J.F. Entrapping intermediates of thermal aggregation in alphahelical proteins with low concentration of guanidine hydrochloride. J Biol Chem. 275:2000;27689-27693.
33. Gomez-Orellana I., Variano B., Miura-Fraboni J., Milstein S., Paton D.R. Thermodynamic characterization of an intermediate state of human growth hormone. Protein Sci. 7:1999;1352-1358.