Instability, stabilization, and formulation of liquid protein pharmaceuticals

International Journal of Pharmaceutics

Volumn 185, Issue 2, 1999, Pages 129-188

  Wang, Wei ^a  

^a BAYER CORPORATION   (United States)

Author keywords

Aggregation; Degradation; Denaturation; Melting; Preferential interaction; Unfolding

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; BASIC FIBROBLAST GROWTH FACTOR; BASIC PROTEIN; BOVINE INSULIN; CHYMOTRYPSINOGEN; COLONY STIMULATING FACTOR 1; DEOXYRIBONUCLEASE; DEOXYRIBONUCLEASE I; DIPHTHERIA TOXOID; ENOLASE; ENZYME; GAMMA UROGASTRONE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GROWTH HORMONE RELEASING FACTOR; HORMONE; KERATINOCYTE GROWTH FACTOR; LYPRESSIN; OXIDOREDUCTASE; PANCREATIC RIBONUCLEASE; PARATHYROID HORMONE; PHOSPHOTRANSFERASE; PLASMINOGEN ACTIVATOR; PROTEIN; PSEUDOMONAS EXOTOXIN; RECOMBINANT PROTEIN; RIBONUCLEASE A; TETANUS TOXOID; THROMBOPOIETIN; UNINDEXED DRUG; VACCINE;

ANALYTIC METHOD; DEAMINATION; DEGLYCOSYLATION; DENATURATION; DRUG FORMULATION; DRUG STABILITY; MELTING POINT; OXIDATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; REVIEW; SOLUTION AND SOLUBILITY;

ANIMALS; CHEMISTRY, PHARMACEUTICAL; DRUG STABILITY; DRUG STORAGE; FREEZE DRYING; HUMANS; PHARMACEUTICAL PREPARATIONS; PROTEINS;

EID: 0032782071     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-5173(99)00152-0     Document Type: Review

References (315)

1. Ackland C.E., Berndt W.G., Frezza J.E., Landgraf B.E., Pritchard K.W., Ciardelli T.L. Monitoring of protein conformation by high-performance size-exclusion liquid chromatography and scanning diode array second-derivative UV absorption spectroscopy. J. Chromatogr. 540:1991;187-198.
2. Adams M.W. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47:1993;627-658.
3. Adams M.W. Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms. FEMS Microbiol. Rev. 15:1994;261-277.
4. Allison S.D., Dong A., Carpenter J.F. Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying and rehydration. Biophys. J. 71:1996;2022-2032.
5. Apenten R.K.O. Protein stability function relations: β-lactoglobulin-A sulphydryl group reactivity and its relationship to protein unfolding stability. Int. J. Biol. Macromol. 23:1998;19-25.
6. Arakawa T., Prestrelski S.J., Kenney W.C., Carpenter J.F. Factors affecting short-term and long term stabilities of proteins. Adv. Drug Deliv. Rev. 10:1993;1-28.
7. Arakawa T., Yoshiko K., Carpenter J.F. Protein-solvent interactions in pharmaceutical formulations. Pharm. Res. 8:1991;285-291.
8. Arnold U., Ulbrich-Hofmann R. Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B. Biochemistry. 36:1997;2166-2172.
9. Aronsson G., Brorsson A.C., Sahlman L., Jonsson B.H. Remarkably slow folding of a small protein. FEBS Lett. 411:1997;359-364.
10. Baek W.O., Vijayalakshmi M.A. Effect of chemical glycosylation of RNase A on the protein stability and surface histidines accessibility in immobilized metal ion affinity electrophoresis (IMAGE) system. Biochim. Biophy. Acta. 1336:1997;394-402.
11. Bai Y., Englander S.W. Future directions in folding: the multi-state nature of protein structure. Proteins Struc. Funct. Genet. 24:1996;145-151.
12. Bai Y., Milne J.S., Mayne L., Englander S.W. Protein stability parameters measured by hydrogen exchange. Proteins Struc. Funct. Genet. 20:1994;4-14.
13. Bam N.B., Cleland J.L., Randolph T.W. Molten globule intermediate of recombinant human growth hormone: stabilization with surfactants. Biotechnol. Prog. 12:1996;801-809.
14. Bam L., Cleland J.L., Yang J., Manning M.C., Carpenter J.F., Kelley R.F., Randolph T.W. Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions. J. Pharm. Sci. 87:1998;1554-1559.
15. Bam N.B., Randolph T.W., Cleland J.L. Stability of protein formulations: investigation of surfactant effects by a novel EPR spectroscopic technique. Pharm. Res. 12:1995;2-11.
16. Baptista A.M., Martel P.J., Petersen S.B. Simulation of protein conformational freedom as a function of pH: constant-pH molecular dynamics using implicit titration. Proteins Struc. Funct. Genet. 27:1997;523-544.
17. Barteri M., Gaudiano M.C., Santucci R. Influence of glycerol on the structure and stability of ferric horse heart myoglobin: a SAXS and circular dichroism study. Biochim. Biophys. Acta. 1295:1996;51-58.
18. Baudyš M., Uchio T., Mix D., Wilson D., Kim S.W. Physical stabilization of insulin by glycosylation. J. Pharm. Sci. 84:1995;28-33.
19. Berry A. Prince N.C. Criteria of protein purity in Proteins. Labfax. 1996;73-84 Academic Press, San Diego, CA.
20. Boctor A.M., Mehta S.C. Enhancement of the stability of thrombin by polyols: microcalorimetric studies. J. Pharm. Pharmacol. 44:1992;600-603.
21. Bond M., Jankowski M., Patel H. et al. Biochemical characterization of recombinant factor IX. Semin. Hematol. 35:1998;11-17.
22. Brange J., Andersen L., Laursen E.D., Meyn G., Rasmussen E. Toward understanding insulin fibrillation. J. Pharm. Sci. 86:1997;517-525.
23. Brange J., Havelund S., Hougaard P. Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations. Pharm. Res. 9:1992;727-734.
24. Brange J., Langkjær L., Havelund S., Vølund A. Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations. Pharm. Res. 9:1992;715-726.
25. Brewster M.E., Hora M.S., Simpkins J.W., Bodor N. Use of 2-hydroxypropyl-β-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs. Pharm. Res. 8:1991;792-795.
26. Brose D.J., Waibel P. Adsorption of proteins to commercial microfiltration capsules. Biopharmocology. 9:1996;36-40.
27. Brunchu S., Forbes R.T., Nyqvist H., York P. A calorimetric study of the effect of cyclodextrins on the thermal stability of lysozyme. Pharm. Res. (Suppl.). 13:1996;S94.
28. Burke C.J., Steadman B.L., Volkin D.B., Tsai P-K., Bruner M.W., Middaugh C.R. The adsorption of proteins to pharmaceutical container surfaces. Int. J. Pharm. 86:1992;89-93.
29. Butler L.G. Enzymes in non-aqueous solvents. Enzyme Microb. Technol. 1:1979;253-259.
30. Butler W.L. Fouth Derivative Spectra. Methods Enzymol. 56:1979;501-515.
31. Caliceti P., Veronese F.M. Successful insulin delivery by PEG conjugation. Proc. Intern. Symp. Control. Rel. Bioact. Mater. 25:1998;263-264.
32. Campbell I.D., Downing A.K. NMR of modular proteins. Nat. Struct. Biol. (Suppl.). 5:1998;496-499.
33. +-dependent bacillar alcohol dehydrogenase. Eur. J. Biochem. 222:1994;345-352.
34. Carpenter J.F., Crowe J.H., Arakawa T. Comparison of solute-induced protein stabilization in aqueous solution and in frozen and dried state. J. Dairy Sci. 73:1990;3627-3636.
35. Carpenter J.F., Pikal M.J., Chang B.S., Randolph T.W. Rational design of stable lyophilized protein formulations: some practical advice. Pharm. Res. 14:1997;969-975.
36. Carr S.A., Hemling M.E., Bean M.F., Roberts G.D. Integration of mass spectrometry in analytical biotechnology. Anal. Chem. 63:1991;2802-2824.
37. Chan H.-K., Au-Yeung K.-L., Gonda I. Effects of additives on heat denaturation of rhDNase in solutions. Pharm. Res. 13:1996;756-761.
38. Chan H.S., Dill K.A. Polymer principles in protein structure and stability. Annu. Rev. Biophy. Chem. 20:1991;447-490.
39. Chang B.S., Beauvais R.M., Arakawa T., Narhi L.O., Dong A., Aparisio D.I., Carpenter J.F. Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution. Biophy. J. 71:1996;3399-3406.
40. Chang B.S., Reeder G., Carpenter J.F. Development of a stable freeze-dried formulation of recombinant human interleukin-1 receptor antagonist. Pharm. Res. 13:1996;243-249.
41. Chang B.S., Randall C.S., Lee Y.S. Stabilization of lyophilized porcine pancreatic elastase. Pharm. Res. 10:1993;1478-1483.
42. Chang N., Hen S.J., Klibanov A.M. Protein separation and purification in neat dimethyl sulfoxide. Biochem. Biophys. Res. Commun. 176:1991;1462-1468.
43. Charm S.E., Wong B.L. Enzyme inactivation with shearing. Biotechnol. Bioeng. 12:1970;1103-1109.
44. Charm S.E., Wong B.L. Shear degradation of fibrinogen in the circulation. Science. 170:1970;466-468.
45. Charman S.A., Mason M.L., Charman W.N. Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone. Pharm. Res. 10:1993;954-962.
46. Charman S.A., Ralph C.E., Bakalova M.V., Charman W.N. The effects of poloxamers 407 and 188 on the conformational stability and aggregation of recombinant porcine growth hormone. Pharm. Res. (Suppl.). 12:1995;S92.
47. Chehin R., Thorolfsson M., Knappskog P.M. et al. Domain structure and stability of human phenylalanine hydroxylase inferred from infrared spectroscopy. FEBS Lett. 422:1998;225-230.
48. Chen B., Costantino H.R., Chung J.L., Hsu C., Shire S.J. The influence of calcium ions on the structure and stability of recombinant human deoxyribonuclease I in the aqueous and lyophilized states. PharmSci (Suppl.). 1:1998;S543.
49. Chen B.-L., Arakawa T., Hsu E., Narhi L.O., Tressel T.J., Chien S.L. Strategies to suppress aggregation of recombinant keratinocyte growth factor during liquid formulation development. J. Pharm. Sci. 83:1994;1657-1661.
50. Chen B-L., Arakawa T., Morris C.F., Kenney W.C., Wells C.M., Pitt C.G. Aggregation pathway of recombinant human keratinocyte growth factor and its stabilization. Pharm. Res. 11:1994;1581-1587.
51. Chiti F., van Nuland N.A.J., Taddei N., Magherini F., Stefani M., Ramponi G., Dobson M. Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH. Biochemistry. 37:1998;1447-1455.
52. Chuyen N.V. Maillard reaction and food processing. Application aspects. Adv. Exp. Med. Biol. 434:1998;213-235.
53. Clarke A.R., Waltho J.P. Protein folding pathways and intermediates. Curr. Opin. Biotechnol. 8:1997;400-410.
54. Cleland J.L., Powell M.F., Shire S.J. The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Ther. Drug Carrier Syst. 10:1993;307-377.
55. Clore G.M., Gronenborn A.M. Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol. 16:1998;22-34.
56. Cooper B.F., Sideraki V., Wilson D.K. et al. The role of divalent cations in structure and function of murine adenosine deaminase. Protein Sci. 6:1997;1031-1037.
57. Cooper E.A., Knutson K. Fourier transform infrared spectroscopy investigations of protein structures. Herron J.N., Jiskoot W., Crommelin D.J.A. Physical Methods to Chracterize Pharmaceutical Proteins. 1995;101-143 Plenum Press, New York.
58. Costantino H.R., Brown S.H., Kelly R.M. Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Prococcus furiosus, exhibiting a temperature optimum of 105 to 115°C. J. Bacteriol. 172:1990;3654-3660.
59. Costantino H.R., Langer R., Klibanov A.M. Solid-phase aggregation of proteins under pharmaceutically relevant conditions. J. Pharm. Sci. 83:1994;1662-1669.
60. Costantino H.R., Langer R., Klibanov A.M. Moisture-induced aggregation of lyophilized insulin. Pharm. Res. 11:1994;21-29.
61. Cowan D.A. Thermophilic proteins: stability and function in aqueous and organic solvent. Comp. Biochem. Physiol. 118A:1997;429-438.
62. Craig D.Q.M., Royall P.G. The use of modulated temperature DSC for the study of pharmaceutical systems: potential uses and limitations. Pharm. Res. 15:1998;1152-1153.
63. Cross R.T., Schirch V. Effect of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptide. J. Biol. Chem. 266:1991;22549-22556.
64. Damodaran S., Song K.B. Kinetics of adsorption of proteins at interfaces: role of protein conformation in diffusional adsorption. Biochim. Biophy. Acta. 954:1988;253-264.
65. Daniel R.M., Dines M., Petach H.H. The denaturation and degradation of stable enzymes at high temperature. Biochem. J. 317:1996;1-11.
66. Darby N., Creighton T.E. Probing protein folding and stability using disulfide bonds. Mol. Biotechnol. 7:1997;57-77.
67. Darnell J., Lodish H., Baltimore D. Introduction: molecules, cells, and experimental technique. Molecular Cell Biology, Part I. 1986;17-266 Scientific American Books, New York.
68. Darrington R.T., Anderson B.D. Evidence for a common intermediate in insulin deamidation and covalent dimer formation: effects of pH and aniline trapping in dilute acidic solutions. J. Pharm. Sci. 84:1995;275-282.
69. D'Auria S., Barone S., Rossi M. et al. Effects of temperature and SDS on the structure of β-glycosidase from the thermophilic archaeon Sulfolobus solfataricus. Biochem. J. 323:1997;833-840.
70. Davio S.R., Kienle K.M., Collins B.E. Interchain interactions in the chimeric protein toxin sCD4(178)-PE40: a differential scanning calorimetry (DSC) study. Pharm. Res. 12:1995;642-648.
71. De Young L.R., Dill K.A., Fink A.L. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry. 32:1993;3877-3886.
72. Dill K.A. Dominant forces in protein folding. Biochemistry. 29:1990;7133-7155.
73. Dill K.A., Alonso D.O.V., Hutchinson K. Thermal stabilities of globular proteins. Biochemistry. 28:1989;5439-5449.
74. Dimitrov R.A., Crichton R.R. Self-consistent field approach to protein structure and stability. 1. pH dependence of electrostatic contribution. Proteins Struc. Funct. Genet. 27:1997;576-596.
75. Dix D.B., Carpenter J.F., Halcome J., Reeder G., Chang B.S. Increasing the physical stability of a hydrophobic protein: rhCNTF. Pharm. Res. (Suppl.). 12:1995;S97.
76. Dobson C.M., Hore P.J. Kinetic studies of protein folding using NMR spectroscopy. Nat. Struct. Biol. 5:1998;504-507.
77. Dong A., Caughey W.S. Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 232:1994;139-175.
78. Dong A., Huang P., Caughey W.S. Protein secondary structures in water from second-derivative amide infrared spectra. Biochemistry. 29:1990;3303-3308.
79. Dong A., Kendrick B., Kreilgård L., Matsuura J., Manning M.C., Carpenter J.F. Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution. Arch. Biochem. Biophy. 347:1997;213-220.
80. Dong A., Matsuura J., Allison S.D., Chrisman E., Manning M.C., Carpenter J.F. Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B. Biochemistry. 35:1995;1450-1457.
81. Dong A., Prestrelski S.J., Allison S.D., Carpenter J.F. Infrared spectroscopic studies of lyophilization- and termperature-induced protein aggregation. J. Pharm. Sci. 84:1995;415-423.
82. Dosztányi Z., Fiser A., Simon I. Stabilization centers in proteins: identification, characterization and predictions. J. Mol. Biol. 272:1997;597-612.
83. Du C., Ye J.M., Wolfe J.L. Improved folding yields of a model protein using protien disulfide isomerase. Pharm. Res. 15:1998;1808-1815.
84. Dyson H.J., Wright P.E. Equilibrium NMR studies of unfolded and partially folded proteins. Nat. Struct. Biol. (Suppl.). 5:1998;499-503.
85. Eckhardt B.M., Oeswein J.Q., Yeung D.A., Milby T.D., Bewley T.A. A turbidimetric method to determine visual appearance of protein solutions. J. Parent. Sci. Technol. 48:1994;64-70.
86. Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:1994;482-501.
87. Evans S., Grassam P. Considerations for parenteral dosage form development of natural alpha interferon. J. Par. Sci. Technol. 40:1986;83-87.
88. Farnsworth P.N., Groth-Vasselli B., Greenfield N.J., Singh K. Effects of temperature and concentration on bovine lens α-crystallin secondary structure: a circular dichroism spectroscopic study. Int. J. Biol. Macromol. 20:1997;283-291.
89. Farruggia B., Garcia G., D'Angelo C., Picó G. Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches. Int. J. Biol. Macromol. 20:1997;43-51.
90. Fatouros A., Österberg T., Mikaelsson M. Recombinant factor VIII SQ - influence of oxygen, metal ions, pH and ionic strength on its stability in aqueous solution. Int. J. Pharm. 155:1997;121-131.
91. Fatouros A., Österberg T., Mikaelsson M. Recombinant factor VIII SQ - inactivation kinetics in aqueous solution and the influence of disaccharides and sugar alcohols. Pharm. Res. 14:1997;1679-1684.
92. Fields G., Alonso D., Stiger D., Dill K. Theory for the aggregation of proteins and copolymers. J. Phys. Chem. 96:1992;3974-3981.
93. Figeys D., Aebersold R. High sensitivity analysis of proteins and peptides by capillary electrophoresis-tandem mass spectrometry: recent developments in technology and applications. Electrophoresis. 19:1998;885-892.
94. Fogliano V., Monti S.M., Visconti A. et al. Identification of a β-lactoglobulin lactosylation site. Biochim. Biophys. Acta. 1388:1998;295-304.
95. Foord R.L., Leatherbarrow R.J. Effect of osmolytes on the exchange rates of backbone amide protons in proteins. Biochemistry. 37:1998;2969-2978.
96. Fransson J., Florin-Robertsson E., Axelsson K., Nyhlén C. Oxidation of human insulin-like growth factor I in formulation studies: kinetics of methionine oxidation in aqueous solution and in solid state. Pharm. Res. 13:1996;1252-1257.
97. Fransson J., Hagman A. Oxidation of human insulin-like growth factor I in formulation sudies. II. Effect of oxygen, visible light, and phosphate on methionine oxidation in aqueous solution and evaluation of possible mechanisms. Pharm. Res. 13:1996;1476-1481.
98. Frye K.J., Royer C.A. The kinetic basis for the stabilization of staphylococcal nuclease by xylose. Protein Sci. 16:1997;789-793.
99. Ganzález M., Murature D.A., Fidelio G.D. Thermal stability of human immunoglobulins with sorbitol. Vox Sang. 68:1995;1-4.
100. Giancola C., De Sena C., Fessas D., Graziano G., Barone G. DSC studies on bovine serum albumin denaturation: effects of ionic strength and SDS concentration. Int. J. Biol. Macromol. 20:1997;193-204.
101. Gianfreda L., Scarfi M.R. Enzyme stabilization: the state of art. Mol. Cell. Biochem. 100:1991;97-128.
102. Gibson T.D. Protein stabilization using additives based on multiple electrostatic interactions. Dev. Biol. Stand. 87:1996;207-217.
103. Gietz U., Alder R., Langguth P., Arvinte T., Merkle H.P. Chemical degradation kinetics of recombinant hirudin (HV1) in aqueous solution: effect of pH. Pharm. Res. 15:1998;1456-1462.
104. Goedken E.R., Marqusee S. Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension. Proteins Struc. Funct. Genet. 33:1998;135-143.
105. Golbik R., Zahn R., Harding S.E., Fersht A.R. Thermodynamic stability and folding of GroEL minichaperones. J. Mol. Biol. 276:1998;505-515.
106. Gombotz W.R., Pankey S.C., Bouchard L.S., Phan D.H., MacKenzie A.P. Stability, characterization, formulation and delivery system development for transforming growth factor-beta1. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;219-245 Plenum Press, New York.
107. Goolcharran C., Borchardt R.T., Keck R., Cleland J.L. Comparison of the rate of deamidation and diketopiperazine formation in rhVEGF and model peptides. PharmSci (Suppl.). 1:1998;S535.
108. Goormaghtigh E., Cabiaux V., Ruysschaert J.-M. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy II. Experimental aspects, side chain structure, and H/D exchange. Subcell. Biochem. 23:1994;363-404.
109. Goormaghtigh E., Cabiaux V., Ruysschaert J.-M. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy III. Secondary structures. Subcell. Biochem. 23:1994;405-450.
110. Goto Y., Fink A.L. Conformational states of β-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry. 28:1989;945-952.
111. Goto Y., Fink A.L. Acid-induced folding of heme proteins. Methods Enzymol. 232:1994;3-15.
112. Griebenow K., Klibanov A.M. Lyophilization-induced reversible changes in the secondary structure of proteins. Proc. Natl. Acad. Sci. USA. 92:1995;10969-10976.
113. Gu L.C., Erdös E.A., Chiang H.-S. et al. Stability of interleukin 1β(IL-1β) in aqueous solution: analytical methods, kinetics, products, and solution formulation implications. Pharm. Res. 8:1991;485-490.
114. Guerra P., Acklin C., Kosky A.A., Davis J.M., Treuheit M.J., Brems D.N. PEGylation prevents the N-terminal degradation of megakaryocyte growth and development factor. Pharm. Res. 15:1998;1822-1827.
115. Hagiwara T., Kumagai H., Nakamura K. Fractal analysis of aggregates formed by heating dilute BSA solutions using light scattering methods. Biosci. Biotechol. Biochem. 60:1996;1757-1763.
116. Heimburg T., Marsh D. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65:1993;2408-2417.
117. Hendrick J.P., Hartl F.-U. The role of molecular chaperones in protein folding. FASEB J. 9:1995;1559-1569.
118. Hensel R., König H. Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49:1988;75-79.
119. Herman A.C., Boone T.C., Lu H.S. Characterization, formulation, and stability of Neupogen® (Filgrastim), a recombinant human granulocyte-colony stimulating factor. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;303-328 Plenum Press, New York.
120. Hsu C.C., Nguyen H.M., Yeung D.A. et al. Surface denaturation at solid-void interface - a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures. Pharm. Res. 12:1995;69-77.
121. Hsu C.C., Ward C.A., Pearlman R., Nguyen H.M., Yeung D.A., Curley J.G. Determining the optimum residual moisture in lyophilized protein pharmaceuticals. Develop. Biol. Stand. 74:1991;255-271.
122. Hu H.Y., Lu Z.X., Du Y.C. Solution conformation of N-terminal fragments of trichosanthin small domain (TCS 182-200) - Circular dichroic studies. J. Pep. Res. 49:1997;113-119.
123. Huber R., Kurr M., Jannasch H.W., Stetter K.O. A novel group of abyssal methanogenic archaebacteria (Methanopyrus) growing at 110°C. Nature. 342:1989;833-834.
124. Hung H.C., Chang G.G. Biphasic denaturation of human placental alkaline phosphatase in guanidinium chloride. Proteins Struc. Funct. Genet. 33:1998;49-61.
125. Ip A.Y., Arakawa T., Silvers H., Ransone C.M., Niven R.W. Stability of recombinant consensus interferon to air-jet and ultrasonic nebulization. J. Pharm. Sci. 84:1995;1210-1214.
126. Jaenicke R. Protein structure and function at low temperatures. Philos. Trans. R. Soc. London B. 326:1990;535-551.
127. Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202:1991;715-728.
128. Jaenicke R. Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: strategies of protein stabilization. FEMS Microbiol. Rev. 18:1996;215-224.
129. 1-antitrypsin polymerization probed by fluorescence spectroscopy. Arch. Biochem. Biophy. 356:1998;296-300.
130. Jensen J.L., Roy S.E., Hershenson S.I., Schöneich C. Metal-catalyzed degradation of brain-derived neurotrophic factor (BDNF): analytical and mechanistic challenges. PharmSci (Suppl.). 1:1998;S536.
131. Jensen W.A., Armstrong J.M., De Giorgio J., Hearn M.T. Stability studies on pig heart mitochondrial malate dehydrogenase: the effect of salts and amino acids. Biochim. Biophys. Acta. 1296:1996;23-34.
132. Jensen W.A., Armstrong J.M., De Giorgio J., Hearn M.T. Thermodynamic analysis of the stabilisation of pig heart mitochondrial malate dehydrogenase and maize leaf phosphoenolpyruvate carboxylase by different salts, amino acids and polyols. Biochim. Biophys. Acta. 1338:1997;186-198.
133. Jensen-Pippo K.E., Whitcomb K.L., Woodward M., Wilson J., Reardon P., Habberfield A. Enteral bioavailability of pegylated IFN-Con1. Pharm. Res. (Suppl.). 12:1995;S291.
134. Johnson B.A., Shirokawa J.M., Hancock W.S., Spellman M.W., Basa L.J., Aswad D.W. Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone. J. Biol. Chem. 264:1989;14262-14271.
135. Johnson C.M., Oliveberg M., Clarke J., Fersht A.R. Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks. J. Mol. Biol. 268:1997;198-208.
136. Johnston T.P. Adsorption of recombinant human granulocyte colony stimulating factor (rhG-CSF) to polyvinyl chloride, polypropylene, and glass: effect of solvent additives. PDA J. Pharm. Sci. Technol. 50:1996;238-245.
137. Jones A.J.S. Analytical Methods for the Assessment of Protein Formulations and Delivery Systems. Cleland J.L., Langer R. Formulation and Delivery of Proteins and Peptides. 1994;23-44 American Chemical Society, Washington DC.
138. Kanazawa H., Fujimoto S., Ohara A. Effect of radical scavengers on the inactivation of papain by ascorbic acid in the presence of cupric ions. Biol. Pharm. Bull. 17:1994;476-481.
139. Katakam M., Banga A.K. Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses. Pharm. Dev. Technol. 2:1997;143-149.
140. Katakam M., Bell L.N., Banga A.K. Effect of surfactants on the physical stability of recombinant human growth hormone. J. Pharm. Sci. 84:1995;713-716.
141. Katre N.V. The conjugation of proteins with polyethylene glycol and other polymers altering properties of proteins to enhance their therapeutic potential. Adv. Drug Del. Rev. 10:1993;91-114.
142. Kaushal P., Burducea I, Hunt S., Geblaoui A., Gentz R., Khan F. Identification of chemical modifications in proteins, myeloid progenitor inhibitory factor-1 (MPIF-1) and keratinocyte growth factor-2 (KGF-2) by matrix-assisted laser desorption mass spectrometry. PharmSci (Suppl.). 1:1998;S537.
143. Kendrick B.S., Chang B.S., Arakawa T. et al. Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state. Proc. Natl. Acad. Sci. USA. 94:1997;11917-11922.
144. Kendrick B.S., Carpenter J.F., Cleland J.L., Randolph T.W. A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma. Proc. Natl. Acad. Sci. USA. 95:1998;14142-14146.
145. Kendrick B.S., Cleland J.L., Lam X. et al. Aggregation of recombinant human interferon gamma: kinetics and structural transitions. J. Pharm. Sci. 87:1998;1069-1076.
146. Kendrick B.S., Dong A., Allison S.D., Manning M.C., Carpenter J.F. Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. J. Pharm. Sci. 85:1996;155-158.
147. Kerwin B.A., Alkers M.J., Apostol I. et al. Acute and long-term stability studies of deoxy hemoglobin and characterization of ascorbate-induced modifications. J. Pharm. Sci. 88:1998;79-88.
148. Khossravi M., Borchardt R.T. Chemical pathways of peptide degradation: IX. Metal-catalyzed oxidation of histidine in model peptides. Pharm. Res. 15:1998;1096-1102.
149. Kita Y., Arakawa T., Lin T-Y., Timasheff S.N. Contribution of the surface energy perturbation to protein-solvent interactions. Biochemistry. 33:1994;15178-15189.
150. Knapp S., Mattson P.T., Christova P. et al. Thermal unfolding of small proteins with SH3 domain folding pattern. Proteins: Struct. Funct. Gen. 31:1998;309-319.
151. Knepp V.M., Whatley J.L., Muchnik A., Calderwood T.S. Identification of antioxidants for prevention of peroxide-mediated oxidation of recombinant human ciliary neurotrophic factor and recombinant human nerve growth factor. J. Pharm. Sci. Technol. 50:1996;163-171.
152. Knepp V.M., Muchnik A., Oldmark S., Kalashnikova L. Stability of nonaqueous suspension formulation of plasma derived factor IX and recombinant human alpha interferon at elevated temperatures. Pharm. Res. 15:1998;1090-1095.
153. Kohn W.D., Kay C.M., Hodges R.S. Salt effects on protein stability: two-stranded alpha-helical coiled-coils containing inter- or intrahelical ion pairs. J. Mol. Biol. 267:1997;1039-1052.
154. Kosa T., Maruyama T., Otagiri M. Species differences of serum albumins: II chemical and thermal stability. Pharm. Res. 15:1998;449-454.
155. Kreilgaard L, Jones L.S., Randolph T.W. et al. Effect of Tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII. J. Pharm. Sci. 87:1998;1597-1603.
156. Kristjánsson M.M., Kinsella J.E. Protein and enzyme stability: structural, thermodynamic, and experimental aspects. Adv. Food Nutr. Res. 35:1991;237-316.
157. Kuhlman B., Yang H.Y., Boice J.A., Fairman R., Raleigh D.P. An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability. J. Mol. Biol. 270:1997;640-647.
158. Kurochkin I.V., Procyk R., Bishop P.D. et al. Domain structure, stability and domain-domain interactions in recombinant factor XIII. J. Mol. Biol. 248:1995;414-430.
159. Kuwata K., Era S., Sogami M. The kinetic studies on the intramolecular SH, S-S exchange reaction of bovine mercaptalbumin. Biophim. Biophys. Acta. 1205:1994;317-324.
160. 1-antitrypsin toward urea denaturation and thermal deactivation. Biophim. Biophys. Acta. 1335:1997;265-272.
161. Lam X.M., Costantino H.R., Overcashier D.E., Nguyen T.H., Hsu C.C. Replacing succinate with glycolate buffer improves the stability of lyophilized interferon-γ Int. J. Pharm. 142:1996;85-95.
162. Lau F.W., Bowie J.U. A method for assessing the stability of a membrane protein. Biochemistry. 36:1997;5884-5892.
163. Lee B., Vasmatzis G. Stabilization of protein structures. Curr. Opin. Biotechnol. 8:1997;423-428.
164. Lewis S.A., Cowan N.J. Progress in understanding protein folding. Pharm. Technol. 20:1996;40-48.
165. Li S., Schöneich C., Wilson G.S., Borchardt R.T. Chemical pathways of peptide degradation. V. Ascorbic acid promotes rather than inhibits the oxidation of methionine to methionine sufoxide in small model peptides. Pharm. Res. 10:1993;1572-1579.
166. Li S., Nguyen T., Schöneich C., Borchardt R.T. Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation. Biochemistry. 34:1995;5762-5772.
167. Li S., Schöneich C., Borchardt R.T. Chemical instability of proteins. Pharm. News. 2:1995;12-16.
168. Li S., Schöneich C., Borchardt R.T. Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization. Biotechnol. Bioeng. 48:1995;491-500.
169. Li S., Patapoff T.W., Nguyen T.H., Borchardt R.T. Inhibitory effect of sugars and polyols on the metal-catalyzed oxidation of human relaxin. J. Pharm. Sci. 85:1996;868-872.
170. Li S., Patapoff T.W., Overcashier D., Hsu C., Nguyen T.H., Borchardt R.T. Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state. J. Pharm. Sci. 85:1996;873-877.
171. Lin L.S., Kunitani M.G., Hora M.S. Interferon-β-1b (Betaseron®): a model for hydrophobic therapeutic proteins. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;275-301 Plenum Press, New York.
172. Lin T.-Y., Timasheff S.N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5:1996;372-381.
173. Lis H., Sharon N. Protein glycosylation-structural and functional aspects. Eur. J. Biochem. 218:1993;1-27.
174. Liu D.T-Y. Glycoprotein pharmaceuticals: scientific and regulatory considerations, and the US Orphan Drug Act. Trends Biotechnol. 10:1992;114-120.
175. Liu J.L., Lu K.V., Eris T. et al. In vitro methionine oxidation of recombinant human leptin. Pharm. Res. 15:1998;632-640.
176. Liu Y., Bolen D.W. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry. 34:1995;12884-12891.
177. Liu Y., Sturtevant J.M. The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding. Biochemistry. 35:1996;3059-3062.
178. Lo Y.L., Rahman Y.E. Effect of lipids on the thermal stability and conformational changes of proteins: ribonuclease A and cytochrome c. Int. J. Pharm. 161:1998;137-148.
179. Lowry C.L., McGeehan G., LeVine H. Metal ion stabilization of the conformation of a recombinant 19-kDa catalytic fragment of human fibroblast collagenase. Proteins. 12:1992;42-48.
180. Lozano P., De Diego T., Iborra J.L. Dynamic structure/function relationships in the alpha-chymotrypsin deactivation process by heat and pH. Eur. J. Biochem. 248:1997;80-85.
181. Maa Y.-F., Hsu C.C. Protein denaturation by combined effect of shear and air-liquid interface. Biotechnol. Bioeng. 54:1997;503-512.
182. Manallack D.T., Andrews P.R., Woods E.F. Design, synthesis, and testing of insulin hexamer-stabilizing agents. J. Med. Chem. 28:1985;1522-1526.
183. Manning M.C., Matsuura J.E., Kendrick B.S. et al. Approaches for increasing the solution stability of proteins. Biotechnol. Bioeng. 48:1995;506-512.
184. Manning M.C., Patel K., Borchardt R.T. Stability of protein pharmaceuticals. Pharm. Res. 6:1989;903-917.
185. Martins L.O., Huber R., Huber H., Stetter K.O., Da Costa M.S., Santos H. Organic solutes in hyperthermophilic Archaea. Appl. Environ. Microbiol. 63:1997;896-902.
186. Martins L.O., Santos H. Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furiosus in response to salinity and temperature. Appl. Environ. Microbiol. 61:1995;3299-3303.
187. Matsumura M., Signor G., Matthews B.W. Substantial increase of protein stability by multiple disulphide bonds. Nature. 342:1989;291-293.
188. Matsuura J.E., Manning M.C. Heat-induced gel formation of β-lactoglobulin: a study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem. 42:1994;1650-1656.
189. Mayr L.M., Schmid F.X. Stabilization of a protein by guanidinium chloride. Biochemistry. 32:1993;7994-7998.
190. McIntosh K.A., Charman W.N., Charman S.A. The application of capillary electrophoresis for monitoring effects of excipients on protein conformation. J. Pharm. Biomed. Anal. 16:1998;1097-1105.
191. Melo E.P., Aires-Barros M.R., Costa S.M., Cabral J.M. Thermal unfolding of proteins at high pH range studied by UV absorbance. J. Biochem. Biophys. Methods. 34:1997;45-59.
192. Middaugh C.R. Biophysical approaches to the pharmaceutical development of proteins. Drug Dev. Ind. Pharm. 16:1990;2635-2654.
193. Mozhaev V.V., Martinek K. Structure-stability relationships in proteins: new approaches to stabilizing enzymes. Enzyme Microb. Technol. 6:1984;50-59.
194. Munson M., Balasubramanian S., Fleming K.G. et al. What makes a protein a protein? Hydrophobic core design that specify stability and structural properties. Protein Sci. 5:1996;1584-1593.
195. Nabuchi Y., Fujiwara E., Ueno K., Kuboniwa H., Asoh Y., Ushio H. Oxidation of recombinant human parathyroid hormone: effect of oxidized position on the biological activity. Pharm. Res. 12:1995;2049-2052.
196. Nguyen D.N., Becker G.W., Riggin R.M. Protein mass spectrometry: applications to analytical biotechnology. J. Chromatogr. A. 705:1995;21-45.
197. Nguyen T.H., Burnier J., Meng W. The kinetics of relaxin oxidation by hydrogen peroxide. Pharm. Res. 10:1993;1563-1571.
198. Nguyen T.H., Shire S.J. Stability and characterization of recombinant human relaxin. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;247-271 Plenum Press, New York.
199. Österberg, T., Fatouros, A., 1994. Oxygen-reduced aqueous solution of factor VIII. International patent WO94/26286.
200. Overcashier D.E., Brooks D.A., Costantino H.R., Hsu C.C. Preparation of excipient-free recombinant human tissue-type plasminogen activator by lyophilization from ammonium bicarbonate solution: an investigation of the two-stage sublimation phenomenon. J. Pharm. Sci. 86:1997;455-459.
201. Pace C.N. Measuring and increasing protein stability. Trends Biotechnol. 8:1990;93-98.
202. Pace C.N., Shirley B.A., McNutt M., Gajiwala K. Forces contributing to the conformational stability of proteins. FASEB J. 10:1996;75-83.
203. Pancoska P., Fabian H., Yoder G., Baumruk V., Keiderling T.A. Protein structural segments and their interconnections derived from optical spectra. Thermal unfolding of ribonuclease T1 as an example. Biochemistry. 35:1996;13094-13106.
204. Paulsen H., Pflughaupt K.-W. Glycosylamines. Pigman W., Horton D., Wander J.D. The Carbohydrates Chemistry and Biochemistry. 1980;881-921 Academic Press, New York.
205. Picó G. Thermodynamic aspects of the thermal stability of human serum albumin. Biochem. Mol. Biol. Int. 36:1995;1017-1023.
206. Picó G.A. Thermal stability of human serum albumin by sodium halide salts. Biochem. Mol. Biol. Int. 38:1996;1-6.
207. Paranandi M.V., Guzzetta A.W., Hancock W.S., Aswad D.W. Deamidation and isoaspartate formation during in vitro aging of recombinant tissue plasminogen activator. J. Biol. Chem. 269:1994;243-253.
208. Patro S., Przybycien T.M. Simulations of reversible protein aggregate and crystal structure. Biophys. J. 70:1996;2888-2902.
209. Peak M.J., Peak J.G., Stevens F.J. et al. The hyperthermophilic glycolytic enzyme enolase in the archaeon, Pyrococcus furiosus: comparison with mesophilic enolases. Arch. Biochem. Biophys. 313:1994;280-286.
210. Perlman R., Nguyen T. Pharmaceutics of protein drugs. J. Pharm. Pharmcol. 44(Suppl 1):1992;178-185.
211. Petukhov M, Kil Y., Kuramitsu S., Lanzov V. Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices. Proteins: Struct. Func. Gen. 29:1997;309-320.
212. Pikal M.J., Dellerman K.M., Roy M.L., Riggin R.M. The effects of formulation variables on the stability of freeze-dried human growth hormone. Pharm. Res. 8:1991;427-436.
213. Pikal M.J., Rigsbee D.R. The stability of insulin in crystalline and amorphous solids: observation of greater stability for the amorphous form. Pharm. Res. 14:1997;1379-1387.
214. Powell M.F. Peptide Stability in Aqueous Parenteral Formulations. Cleland J.L., Langer R. Formulation and Delivery of Proteins and Peptides. 1994;101-117 American Chemical Society, Washington DC.
215. Powell M.F. A compendium and hydropathy/flexibility analysis of common reactive sites in proteins: Reactivity at Asn, Asp, Gln, and Met motifs in neutral pH solution. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;1-140 Plenum Press, New York.
216. Prehoda K.E., Mooberry E.S., Markley J.L. Pressure denaturation of proteins: evaluation of compressibility effects. Biochemistry. 37:1998;5785-5790.
217. Prestrelski S.J., Arakawa T., Carpenter J.F. Separation of freezing and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy. Arch. Biochem. Biophys. 303:1993;465-473.
218. Prestrelski S.J., Tedeschi N., Arakawa T., Carpenter J.F. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophy. J. 65:1993;661-671.
219. Prestrelski S.J., Pikal K.A., Arakawa T. Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier-transform infrared spectroscopy. Pharm. Res. 12:1995;1250-1259.
220. Prieto J., Wilmans M., Jimenez M.A., Rico M., Serrano L. Non-native local interactions in protein folding and stability: introducing a helical tendency in the all β-sheet α-spectrin SH3 domain. J. Mol. Biol. 268:1997;760-778.
221. Querol E., Pervez-Pons J.A., Mozo-Villarias A. Analysis of protein conformational characteristics related to thermostability. Protein Eng. 9:1996;265-271.
222. Ragone R., Facchiano F., Facchiano A., Facchiano A.M., Colonna G. Flexibility plot of proteins. Protein Eng. 2:1989;497-504.
223. Ramakrishnan V., Verhagen M.F.J.M., Adams M.W.W. Characterization of di-myo-inositol-1,1′-phosphate in the hyperthermophilic bacterium Thermotoga maritina. Appl. Environ. Microbiol. 63:1997;347-350.
224. Raman B., Ramakrishna T., Rao C.M. Effect of the chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease A. FEBS Lett. 416:1997;369-372.
225. Ramos A., Raven N.D.H., Sharp R.J. et al. Stabilization of enzymes against thermal stress and freeze-drying by mannosylglycerate. Appl. Environ. Microbiol. 63:1997;4020-4025.
226. Raschke T.M., Marqusee S. Hydrogen exchange studies of protein structure. Curr. Opin. Biotechnol. 9:1998;80-86.
227. Reid D.G., MacLachlan L.K., Edwards A.J., Hubbard J.A., Sweeney P.J. Introduction to the NMR of proteins. Methods Mol. Biol. 60:1997;1-28.
228. Remmele Jr R.L., Nightlinger N.S., Srinivasan S., Gombotz W.R. Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm. Res. 15:1998;200-208.
229. Richards F.M. Protein stability: still an unsolved problem. Cell. Mol. Life Sci. 53:1997;790-802.
230. Roefs S.P.F.M., De Kruif K.G. A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 226:1994;883-889.
231. Royall P.G., Craig D.Q.M., Doherty C. Characterization of the glass transition of an amorphous drug using modulated DSC. Pharm. Res. 15:1998;1117-1121.
232. Ruddon R.W., Bedows E. Assisted protein folding. J. Biol. Chem. 272:1997;3125.
233. Runkel L., Meier W., Pepinsky R.B. et al. Structural and functional differences between glycosylated and non-glycosylated forms of human interferon-β (IFN-β). Pharm. Res. 15:1998;641-649.
234. Rupley J.A., Careri G. Protein hydration and function. Adv. Protein Chem. 41:1991;37-173.
235. Sanyal G., Marquis-Omer D., Middaugh C.R. Biological characterization and formulation of TP40: a chimeric protein that requires a pH-dependent conformational change for its biological activity. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;365-392 Plenum Press, New York.
236. Sasaoki K., Hiroshima T., Kusumoto S., Nishi K. Deamidation at asparagine-88 in recombinant human interleukin 2. Chem. Pharm. Bull. 40:1992;976-980.
237. Schrier J.A., Kenley R.A., Williams R., Corcoran R.J., Kim Y., Northey R.P. Jr., D'Augusta D., Huberty M. Degradation pathways for recombinant human macrophage colony-stimulating factor in aqueous solution. Pharm. Res. 10:1993;933-944.
238. Schwendeman S.P., Costantino H.R., Gupta R.K., Siber G.R., Klibanov A.M., Langer R. Stabilization of tetanus and diphtheria toxoids against moisture-induced aggregation. Proc. Natl. Acad. Sci. USA. 92:1995;11234-11238.
239. Sendak R.A., Rothwarf D.M., Wedemeyer W.J., Houry W.A., Scheraga H.A. Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A. Biochemistry. 35:1996;12978-12992.
240. Senderoff R.I., Kontor K.M., Heffernan J.K. et al. Aqueous stability of recombinant human thrombopoietin as a function of processing schemes. J. Pharm. Sci. 85:1996;749-752.
241. Shahrokh Z., Beylin I., Eberlein G. et al. Cellulose-cleaving activity contaminating E.coli-produced recombinant proteins. Biopharm. 8:1995;32-38.
242. Shahrokh Z., Eberlein G., Buckley D. et al. Major degradation products of basic fibroblast growth factor: detection of succinimide and iso-aspartate in place of aspartate. Pharm. Res. 11:1994;936-944.
243. Shahrokh Z., Strantton P.R., Eberlein G.A., Wang Y.J. Approaches to analysis of aggregates and demonstrating mass balance in pharmaceutical protein (basic fibroblast growth factor) formulations. J. Pharm. Sci. 83:1994;1645-1649.
244. Shire S.J. Stability characterization and formulation development of recombinant human deoxyribonuclease I [Pulmozyme®, (dornase alpha)]. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;393-426 Plenum Press, New York.
245. Shirley B., Stanssens P., Steyaert J., Pace C.N. Conformational stability and activity of ribonuclease T1 and mutants. J. Biol. Chem. 264:1989;11621-11625.
246. Shoichet B.K., Baase W.A., Kuroki R., Matthews B.W. A relationship between protein stability and protein function. Proc. Natl. Acad. Sci. USA. 92:1995;452-456.
247. Shortle D. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10:1996;27-34.
248. Sindelar C.V., Hendsch Z.S., Tidor B. Effects of salt bridges on protein structure and design. Protein Sci. 7:1998;1898-1914.
249. Sluzky V., Tamada J.A., Klibanov A.M., Langer R. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc. Natl. Acad. Sci. USA. 88:1991;9377-9381.
250. Sluzky V., Klibanov A.M., Langer R. Mechanism of insulin aggregation and stabilization in agitated aqueous solutions. Biotechnol. Bioeng. 40:1992;895-903.
251. Son K., Kwon C. Stabilization of human epidermal growth factor (hEGF) in aqueous formulation. Pharm. Res. 12:1995;451-454.
252. Speed M.A., Wang D.I.C., King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nature Biotechnol. 14:1996;1283-1287.
253. Stadtman E.R. Oxidation of free amino acid residues in proteins by metal-catalyzed reactions. Annu. Rev. Biochem. 62:1993;797-821.
254. Staniforth R.A., Bigotti M.G., Cutruzzola F., Allocatelli C.T. Brunori M unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding. J. Mol. Biol. 275:1998;133-148.
255. Stephenson R.C., Clarke S. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 264:1989;6164-6170.
256. Stevenson C.L., Friedman A.R., Kubiak T.M., Donlan M.E., Borchardt R.T. Effect of secondary structure on the rate of deamidation of several growth hormone releasing factor analogs. Int. J. Peptide Protein Res. 42:1993;497-503.
257. Strickley R.G., Anderson B.D. Solid-state stability of human insulin. I. Mechanism and the effect of water on the kinetics of degradation in lyophiles from pH 2-5 solutions. Pharm. Res. 13:1996;1142-1153.
258. Strickley R.G., Anderson B.D. Solid-state stability of human insulin. II. Effect of water on reactive intermediate partitioning in lyophiles from pH 2-5 solutions: stabilization against covalent dimer formation. J. Pharm. Sci. 86:1997;645-653.
259. Surewicz W., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:1993;389-393.
260. Susi H., Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130:1986;290-311.
261. Swietnicki W., Petersen R., Gambetti P., Surewicz W.K. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272:1997;27517-27520.
262. Takano K, Yamagata Y., Yutani K. A general rule for the relationship between hydrophobic effect and conformational stability of a protein: Stability and structure of a series of hydrophobic mutants of human lysozyme. J. Mol. Biol. 280:1998;749-761.
263. Tandon S., Horowitz P.M. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. J. Biol. Chem. 262:1987;4486-4490.
264. Tang K.E.S., Dill K.A. Native protein fluctuations: The conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J. Biomol. Struct. Dyn. 16:1998;397-411.
265. Tanner J.W., Eckenhoff R.G., Liebman P.A. Halothane, an inhalational anesthetic agent, increases folding stability of serum albumin. Biophim. Biophys. Acta. 1430:1999;46-56.
266. Tarelli E., Corran P.H., Bingham B.R., Mollison H., Wait R. Lysine vasopressin undergoes rapid glycation in the presence of reducing sugars. J. Pharm. Biomed. Anal. 12:1994;1355-1361.
267. Thomson J.A., Shirley B., Grimsley G.R., Pace C.N. Conformational stability and mechanism of folding of ribonuclease T1. J. Biol. Chem. 264:1989;11614-11620.
268. Thurow H., Geisen K. Stabilization of dissolved proteins against denaturation at hydrophobic interfaces. Diabetologia. 27:1984;212-218.
269. Timasheff S.N. Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. Biochemistry. 31:1992;9857-9864.
270. Timasheff S.N. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophy. Biomol. Struct. 22:1993;67-97.
271. Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51:1998;355-432.
272. Topham C.M., Srinivasan N., Blundell T.L. Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables. Protein. Eng. 10:1997;7-21.
273. Townsend M.W., DeLuca P.P. Stability of ribonuclease A in solution and the freeze-dried state. J. Pharm. Sci. 79:1990;1083-1086.
274. Tsai P.K., Volkin D.B., Dabora J.M. et al. Formulation design of acidic fibroblast growth factor. Pharm. Res. 10:1993;649-659.
275. Tsai A.M., van Zanten J.H., Betenbaugh M.J. I. Study of protein aggregation due to heat denaturation: a structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering. Biotechnol. Bioeng. 59:1998;273-280.
276. Tsai A.M., van Zanten J.H., Betenbaugh M.J. II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design. Biotechnol. Bioeng. 59:1998;281-285.
277. + -ATPase from etiolated mung bean seedlings. J. Protein Chem. 17:1998;161-172.
278. Tsutsumi Y., Kihira T., Tsunoda S-I. et al. Polyethylene glycol modification of interleukin-6 enhances its thrombopoietic activity. J. Control. Release. 33:1995;447-451.
279. Tuena de Gómez-Puyou M., Gómez-Puyou A. Enzymes in low water systems. Crit. Rev. Biochem. Mol. Biol. 33:1998;53-89.
280. Tzannis S.T., Hrushesky W.J.M., Wood P.A., Przybycien T.M. Irreversible inactivation of interleukin 2 in a pump-based delivery environment. Proc. Natl. Acad. Sci. USA. 93:1996;5460-5465.
281. Tzannis S.T., Hrushesky W.J.M., Wood P.A., Przybycien T.M. Adsorption of a formulated protein on a drug delivery device surface. J. Colloid Interface Sci. 189:1997;216-228.
282. Vermeer A.W., Bremer M.G., Norde W. Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy. Biochim. Biophys. Acta. 1425:1998;1-12.
283. Vieille C., Zeikus J.G. Thermoenzymes: identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 14:1996;183-191.
284. Vogt G., Argos P. Protein thermal stability: hydrogen bonds or internal packing? Fold. Des. 2:1997;S40-46.
285. Vogt G., Woell S., Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:1997;631-643.
286. Volkin D.B., Burke C.J., Sanyal G., Middaugh C.R. Analysis of vaccine stability. Dev. Biol. Stand. 87:1996;135-142.
287. Volkin D.B., Klibanov A.M. Thermal destruction processes in proteins involving cystine residues. J. Biol. Chem. 262:1987;2945-2950.
288. Volkin D.B., Klibanov A.M. Minimizing protein inactivation. Creighton T.E. Protein Function A Practical Approach. 1989;1-24 Information Press, Oxford, UK.
289. Volkin D.B., Middaugh C.R. The characterization, stabilization, and formulation of acidic fibroblast growth factor. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;181-217 Plenum Press, New York.
290. Volkin D.B., Tsai P.K., Dabora J.M. et al. Physical stabilization of acidic fibroblast growth factor by polyanions. Arch. Biochem. Biophys. 300:1993;30-41.
291. Vrkljan M., Foster T.M., Powers M.E. et al. Thermal stability of low molecular weight urokinase during heat treatment. Part 2. Effect of polymeric additives. Pharm. Res. 11:1994;1004-1008.
292. Wang A., Robertson A.D., Bolen D.W. Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry. 34:1995;15069-15104.
293. Wang C., Eufemi M., Turano C., Giartosio A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry. 35:1996;7299-7307.
294. Wang P-L., Johnston T.P. Enhanced stability of two model proteins in an agitated solution environment using poloxamer 407. J. Parenter. Sci. Technol. 47:1993;183-189.
295. Wang P-L., Johnston T.P. Thermal-induced denaturation of two model proteins: effect of poloxamer 407 on solution stability. Int. J. Pharm. 96:1993;41-49.
296. Wang W. Oral protein drug delivery. J. Drug Target. 4:1996;195-232.
297. Wang Y.J., Shahrokh Z., Vemuri S., Eberlein G., Beylin I., Busch M. Charaterization, stability, and formulation of basic fibroblast growth factor. Pearlman R., Wang Y.J. Formulation, Characterization, and Stability of Protein Drugs. 1996;141-180 Plenum Press, New York.
298. Wen J., Arakawa T., Philo J.S. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240:1996;155-166.
299. Won C.M., Molnar T.E., McKean R.E., Spenlehauer G.A. Stabilizers against heat-induced aggregation of RPR 114849, an acidic fibroblast growth factor (AFGF). Int. J. Pharm. 167:1998;25-36.
300. Wong D., Parascrampuria J. Pharmaceutical excipients for the stabilization of proteins. Pharm. Technol. 21:1997;34-50.
301. Wrabl J.O., Shortle D. Perturbations of the denatured state ensemble: modeling their effects on protein stability and folding kinetics. Protein. Sci. 5:1996;2343-2352.
302. Xie G., Timasheff S.N. Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured than for the native protein. Protein Sci. 6:1997;211-221.
303. Xie G., Timasheff S.N. The thermodynamic mechanism of protein stabilization by trehalose. Biophys. Chem. 64:1997;25-43.
304. Xu G.Y., Yu H.A., Hong J. et al. Solution structure of recombinant human interleukin-6. J. Mol. Biol. 268:1997;468-481.
305. Xie M., Schowen R. Secondary structure and protein deamidation. J. Pharm. Sci. 88:1999;8-13.
306. Yang A-S., Honig B. On the pH dependence of protein stability. J. Mol. Biol. 231:1993;459-474.
307. Yeo S-D., Debenedetti P.G., Patro S.Y., Przybycien T.M. Secondary structure characterization of microparticulate insulin powders. J. Pharm. Sci. 83:1994;1651-1656.
308. Yoshioka S., Aso Y., Izutsu K., Terao T. Aggregates formed during storage of β-galactosidase in solution and in the freeze-dried state. Pharm. Res. 10:1993;103-108.
309. Yoshioka S., Aso Y., Izutsu K., Kojima S. Is stability prediction possible for protein drugs? Denaturation kinetics of β-galactosidase in solution. Pharm. Res. 11:1994;1721-1725.
310. Yoshioka S., Aso Y., Izutsu K-I., Terao T. Application of accelerated testing for shelf-life prediction of commercial protein preparations. J. Pharm. Sci. 83:1994;454-456.
311. Yoshioka S., Aso Y., Kojima S. Softening temperature of lyophilized serum albumin and γ-globulin as measured by spin-spin relaxation time of protein protons. J. Pharm. Sci. 86:1997;470-474.
312. Yoshioka S., Aso Y., Nakai Y., Kojima S. Effect of high molecular mobility of poly(vinyl alcohol) on protein stability of lyophilized γ-globulin formulations. J. Pharm. Sci. 87:1998;147-151.
313. Zhang J., Peng X., Jonas A., Jonas J. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry. 34:1995;8631-8641.
314. Zhao F., Ghezzo-Schöneich E., Aced G.I., Hong J., Milby T., Schöneich C. Metal-catalyzed oxidation of histidine in human growth hormone. J. Biol. Chem. 272:1997;9019-9029.
315. Zhao F., Yang J., Schöneich C. Effects of polyaminocarboxylate metal chelators on iron-thiolate induced oxidation of methionine- and histidine-containing peptides. Pharm. Res. 13:1996;931-938.