메뉴 건너뛰기




Volumn 20, Issue 9, 2003, Pages 1325-1336

Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation

Author keywords

Conformational stability; Denaturation; Formulation; Pharmaceuticals; Second virial coefficient

Indexed keywords

DEOXYHEMOGLOBIN; INSULIN; INTERLEUKIN 1BETA; LOW MOLECULAR WEIGHT PLASMINOGEN ACTIVATOR; RECOMBINANT BLOOD CLOTTING FACTOR 8; RECOMBINANT CONSENSUS INTERFERON; RECOMBINANT GAMMA INTERFERON; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT PROTEIN; RELAXIN; RIBONUCLEASE A; STREPTOKINASE; UNCLASSIFIED DRUG;

EID: 0141567459     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1025771421906     Document Type: Review
Times cited : (1202)

References (111)
  • 1
    • 0001189175 scopus 로고
    • Studies on the denaturation of proteins, XIII. A theory of denaturation
    • H. Wu. Studies on the denaturation of proteins, XIII. A theory of denaturation. Chinese J. Physiol. 5:321-344 (1931).
    • (1931) Chinese J. Physiol. , vol.5 , pp. 321-344
    • Wu, H.1
  • 2
    • 0028948518 scopus 로고
    • Hsien Wu and the first theory of protein denaturation (1931)
    • J. T. Edsall. Hsien Wu and the first theory of protein denaturation (1931). Adv. Protein Chem. 46:1-5 (1995).
    • (1995) Adv. Protein Chem. , vol.46 , pp. 1-5
    • Edsall, J.T.1
  • 3
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • R. Lumry and H. Eyring. Conformation changes of proteins. J. Phys. Chem. 58:110-120 (1954).
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 5
    • 0027729733 scopus 로고
    • The development of stable protein formulations - A close look at protein aggregation, deamidation and oxidation
    • J. L. Cleland, M. F. Powell, and S. J. Shire. The development of stable protein formulations - a close look at protein aggregation, deamidation and oxidation. Crit. Rev. Ther. Drug 10:307-377 (1993).
    • (1993) Crit. Rev. Ther. Drug , vol.10 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 8
    • 0013366578 scopus 로고    scopus 로고
    • Physical stability of proteins
    • S. Frokjaer and L. Hovgaards (eds.), Taylor and Francis, London
    • J. Brange. Physical stability of proteins. In S. Frokjaer and L. Hovgaards (eds.), Pharmaceutical Formulation and Development of Peptides and Proteins, Taylor and Francis, London, 2000, pp. 89-112.
    • (2000) Pharmaceutical Formulation and Development of Peptides and Proteins , pp. 89-112
    • Brange, J.1
  • 10
    • 3242708369 scopus 로고    scopus 로고
    • Surfactant-protein interactions
    • J. F. Carpenter and M. C. Mannings (eds.), Kluwer Academic/Plenum Publishers, New York
    • T. W. Randolph and L. S. Jones. Surfactant-protein interactions. In J. F. Carpenter and M. C. Mannings (eds.), Rational Design of Stable Protein Formulations, Theory and Practice, Kluwer Academic/Plenum Publishers, New York, 2002, p. 198.
    • (2002) Rational Design of Stable Protein Formulations, Theory and Practice , pp. 198
    • Randolph, T.W.1    Jones, L.S.2
  • 11
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation
    • A. C. Dong, S. J. Prestrelski, S. D. Allison, and J. F. Carpenter. Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation. J. Pharm. Sci. 84:415-424 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.C.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 12
    • 0028787409 scopus 로고
    • Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease-a
    • A. Wang, A. D. Robertson, and D. W. Bolen. Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease-a. Biochemistry 34:15096-15104 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15096-15104
    • Wang, A.1    Robertson, A.D.2    Bolen, D.W.3
  • 14
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • A. L. Fink. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold. Des. 3:R9-R23 (1998).
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 16
    • 0030606850 scopus 로고    scopus 로고
    • Aggregation of recombinant human growth hormone induced by phenolic compounds
    • Y. F. Maa and C. C. Hsu. Aggregation of recombinant human growth hormone induced by phenolic compounds. Int. J. Pharm. 140:155-168 (1996).
    • (1996) Int. J. Pharm. , vol.140 , pp. 155-168
    • Maa, Y.F.1    Hsu, C.C.2
  • 17
    • 0037150072 scopus 로고    scopus 로고
    • Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition
    • S. Krishnan, E. Y. Chi, J. N. Webb, B. S. Chang, D. Shan, M. Goldenberg, M. C. Manning, T. W. Randolph, and J. F. Carpenter. Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition. Biochemistry 41:6422-6431 (2002).
    • (2002) Biochemistry , vol.41 , pp. 6422-6431
    • Krishnan, S.1    Chi, E.Y.2    Webb, J.N.3    Chang, B.S.4    Shan, D.5    Goldenberg, M.6    Manning, M.C.7    Randolph, T.W.8    Carpenter, J.F.9
  • 20
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • E. Y. Chi, S. Krishnan, B. S. Kendrick, B. S. Chang, J. F. Carpenter, and T. W. Randolph. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci. 12:903-913 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 21
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • K. A. Dill. Dominant forces in protein folding. Biochemistry 29: 7133-7155 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 22
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • C. N. Pace, B. A. Shirley, M. McNutt, and K. Gajiwala. Forces contributing to the conformational stability of proteins. FASEB J. 10:75-83 (1996).
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 23
    • 0013596465 scopus 로고
    • R. Huber and E. L. Winnackers (eds.), Springer Verlag, Berlin
    • R. Jaenicke. In R. Huber and E. L. Winnackers (eds.), Protein Structure and Protein Engineering, Springer Verlag, Berlin, 1988, pp. 16-36.
    • (1988) Protein Structure and Protein Engineering , pp. 16-36
    • Jaenicke, R.1
  • 25
    • 0025876740 scopus 로고
    • Protein folding: Local structures, domains, subunits, and assemblies
    • R. Jaenicke. Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30:3147-3161 (1991).
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 27
    • 0030882055 scopus 로고    scopus 로고
    • A reassessment of the molecular origin of cold denaturation
    • Tokyo
    • G. Graziano, F. Catanzano, A. Riccio, and G. Barone. A reassessment of the molecular origin of cold denaturation. J. Biochem. (Tokyo) 122:395-401 (1997).
    • (1997) J. Biochem. , vol.122 , pp. 395-401
    • Graziano, G.1    Catanzano, F.2    Riccio, A.3    Barone, G.4
  • 30
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • P. L. Privalov and S. J. Gill. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39:191-234 (1988).
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 31
    • 0035895356 scopus 로고    scopus 로고
    • Polar group burial contributes more to protein stability than nonpolar group burial
    • C. N. Pace. Polar group burial contributes more to protein stability than nonpolar group burial. Biochem. 40:310-313 (2001).
    • (2001) Biochem. , vol.40 , pp. 310-313
    • Pace, C.N.1
  • 32
    • 0039723136 scopus 로고    scopus 로고
    • Minimization of recombinant human flt3 ligand aggregation at the t-m plateau: A matter of thermal reversibility
    • R. L. Remmele, S. D. Bhat, D. H. Phan, and W. R. Gombotz. Minimization of recombinant human flt3 ligand aggregation at the t-m plateau: A matter of thermal reversibility. Biochem. 38:5241-5247 (1999).
    • (1999) Biochem. , vol.38 , pp. 5241-5247
    • Remmele, R.L.1    Bhat, S.D.2    Phan, D.H.3    Gombotz, W.R.4
  • 33
    • 0036037356 scopus 로고    scopus 로고
    • Unfolding and aggregation during the thermal denaturation of streptokinase
    • A. I. Azuaga, C. M. Dobson, P. L. Mateo, and F. Conejero-Lara. Unfolding and aggregation during the thermal denaturation of streptokinase. Eur. J. Biochem. 269:4121-4133 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4121-4133
    • Azuaga, A.I.1    Dobson, C.M.2    Mateo, P.L.3    Conejero-Lara, F.4
  • 34
    • 0028588599 scopus 로고
    • Strategies to suppress aggregation of recombinant keratinocyte growth-factor during liquid formulation development
    • B. L. Chen, T. Arakawa, E. Hsu, L. O. Narhi, T. J. Tressel, and S. L. Chien. Strategies to suppress aggregation of recombinant keratinocyte growth-factor during liquid formulation development. J. Pharm. Sci. 83: 1657-1661 (1994).
    • (1994) J. Pharm. Sci. , vol.83 , pp. 1657-1661
    • Chen, B.L.1    Arakawa, T.2    Hsu, E.3    Narhi, L.O.4    Tressel, T.J.5    Chien, S.L.6
  • 35
    • 0027987422 scopus 로고
    • Aggregation pathway of recombinant human keratinocyte growth- factor and its stabilization
    • B. L. Chen, T. Arakawa, C. F. Morris, W. C. Kenney, C. M. Wells, and C. G. Pitt. Aggregation pathway of recombinant human keratinocyte growth- factor and its stabilization. Pharm. Res. 11:1581-1587 (1994).
    • (1994) Pharm. Res. , vol.11 , pp. 1581-1587
    • Chen, B.L.1    Arakawa, T.2    Morris, C.F.3    Kenney, W.C.4    Wells, C.M.5    Pitt, C.G.6
  • 36
    • 0029134661 scopus 로고
    • Stability of recombinant consensus interferon to air-jet and ultrasonic nebulization
    • A. Y. Ip, T. Arakawa, H. Silvers, C. M. Ransone, and R. W. Niven. Stability of recombinant consensus interferon to air-jet and ultrasonic nebulization. J. Pharm. Sci. 84:1210-1214 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 1210-1214
    • Ip, A.Y.1    Arakawa, T.2    Silvers, H.3    Ransone, C.M.4    Niven, R.W.5
  • 37
    • 0024318970 scopus 로고
    • pH-dependence of the reversible and irreversible thermal-denaturation of gamma-interferons
    • M. G. Mulkerrin and R. Wetzel. pH-dependence of the reversible and irreversible thermal-denaturation of gamma-interferons. Biochem. 28:6556-6561 (1989).
    • (1989) Biochem. , vol.28 , pp. 6556-6561
    • Mulkerrin, M.G.1    Wetzel, R.2
  • 38
    • 0032486768 scopus 로고    scopus 로고
    • II. Electrostatic effect in the aggregation of heat-denatured RNase a and implications for protein additive design
    • A. M. Tsai, J. H. van Zanten, and M. J. Betenbaugh. II. Electrostatic effect in the aggregation of heat-denatured RNase a and implications for protein additive design. Biotechnol. Bioeng. 59:281-285 (1998).
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 281-285
    • Tsai, A.M.1    Van Zanten, J.H.2    Betenbaugh, M.J.3
  • 39
    • 0032486770 scopus 로고    scopus 로고
    • I. Study of protein aggregation due to heat denaturation: A structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering
    • A. M. Tsai, J. H. van Zanten, and M. J. Betenbaugh. 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. 59:273-280 (1998).
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 273-280
    • Tsai, A.M.1    Van Zanten, J.H.2    Betenbaugh, M.J.3
  • 40
    • 0003516749 scopus 로고
    • W. H. Freeman and Company, New York
    • P. Atkins. Physical Chemistry, W. H. Freeman and Company, New York, 1994.
    • (1994) Physical Chemistry
    • Atkins, P.1
  • 41
    • 0030765942 scopus 로고    scopus 로고
    • Recombinant factor VIII SQ - Influence of oxygen, metal ions, ph and ionic strength on its stability in aqueous solution
    • A. Fatouros, T. Osterberg, and M. Mikaelsson. Recombinant factor VIII SQ - influence of oxygen, metal ions, ph and ionic strength on its stability in aqueous solution. Int. J. Pharm. 155:121-131 (1997).
    • (1997) Int. J. Pharm. , vol.155 , pp. 121-131
    • Fatouros, A.1    Osterberg, T.2    Mikaelsson, M.3
  • 43
    • 0030337902 scopus 로고    scopus 로고
    • Stability and characterization of recombinant human relaxin
    • R. Pearlman and Y. J. Wangs (eds.), Plenum Press, New York
    • T. H. Nguyen and S. J. Shire. Stability and characterization of recombinant human relaxin. In R. Pearlman and Y. J. Wangs (eds.), Formulation, Characterization, and Stability of Protein Drugs, Plenum Press, New York, 1996, pp. 247-211.
    • (1996) Formulation, Characterization, and Stability of Protein Drugs , pp. 247-211
    • Nguyen, T.H.1    Shire, S.J.2
  • 45
    • 0025890206 scopus 로고
    • Stability of interleukin-1-beta (IL-1-gamma) in aqueous solution - Analytical methods, kinetics, products, and solution formulation implications
    • L. C. Gu, E. A. Erdos, H. S. Chiang, T. Calderwood, K. Tsai, G. C. Visor, J. Duffy, W. C. Hsu, and L. C. Foster. Stability of interleukin-1-beta (IL-1-gamma) in aqueous solution - analytical methods, kinetics, products, and solution formulation implications. Pharm. Res. 8:485-490 (1991).
    • (1991) Pharm. Res. , vol.8 , pp. 485-490
    • Gu, L.C.1    Erdos, E.A.2    Chiang, H.S.3    Calderwood, T.4    Tsai, K.5    Visor, G.C.6    Duffy, J.7    Hsu, W.C.8    Foster, L.C.9
  • 46
    • 0025226183 scopus 로고
    • Stability of ribonuclease-a in solution and the freeze-dried state
    • M. W. Townsend and P. P. Deluca. Stability of ribonuclease-a in solution and the freeze-dried state. J. Pharm. Sci. 79:1083-1086 (1990).
    • (1990) J. Pharm. Sci. , vol.79 , pp. 1083-1086
    • Townsend, M.W.1    Deluca, P.P.2
  • 47
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • L. Nielsen, R. Khurana, A. Coats, S. Frokjaer, J. Brange, S. Vyas, V. N. Uversky, and A. L. Fink. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry 40:6036-6046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 48
    • 0034633994 scopus 로고    scopus 로고
    • Contribution of salt bridges near the surface of a protein to the conformational stability
    • K. Takano, K. Tsuchimori, Y. Yamagata, and K. Yutani. Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry 39:12375-12381 (2000).
    • (2000) Biochemistry , vol.39 , pp. 12375-12381
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 51
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • S. N. Timasheff. Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Adv. Protein Chem. 51:355-432 (1998).
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 53
    • 0025823103 scopus 로고
    • Dimerization of human growth-hormone by zinc
    • B. C. Cunningham, M. G. Mulkerrin, and J. A. Wells. Dimerization of human growth-hormone by zinc. Science 253:545-548 (1991).
    • (1991) Science , vol.253 , pp. 545-548
    • Cunningham, B.C.1    Mulkerrin, M.G.2    Wells, J.A.3
  • 55
    • 0030727624 scopus 로고    scopus 로고
    • The hofmeister series: Salt and solvent effects on interfacial phenomena
    • M. G. Cacace, E. M. Landau, and J. J. Ramsden. The hofmeister series: Salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 30:241-277 (1997).
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 56
    • 0020477017 scopus 로고
    • Stabilization of protein-structure by sugars
    • T. Arakawa and S. N. Timasheff. Stabilization of protein-structure by sugars. Biochemistry 21:6536-6544 (1982).
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 57
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • J. C. Lee and S. N. Timasheff. The stabilization of proteins by sucrose. J. Biol. Chem. 256:7193-7201 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 58
    • 0029108966 scopus 로고
    • Use of glycerol, polyols, and other protein structure stabilizing agents in protein crystallization
    • R. Sousa. Use of glycerol, polyols, and other protein structure stabilizing agents in protein crystallization. Acta Cryst. D51:271-277 (1995).
    • (1995) Acta Cryst. , vol.D51 , pp. 271-277
    • Sousa, R.1
  • 59
    • 0031660957 scopus 로고    scopus 로고
    • Effects of tween 80 and sucrose on acute short-term stability and long-term storage at - 20 degrees C of a recombinant hemoglobin
    • B. A. Kerwin, M. C. Heller, S. H. Levin, and T. W. Randolph. Effects of tween 80 and sucrose on acute short-term stability and long-term storage at -20 degrees C of a recombinant hemoglobin. J. Pharm. Sci. 87:1062-1068 (1998).
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1062-1068
    • Kerwin, B.A.1    Heller, M.C.2    Levin, S.H.3    Randolph, T.W.4
  • 60
    • 0036167323 scopus 로고    scopus 로고
    • A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20
    • S. D. Webb, J. L. Cleland, J. F. Carpenter, and T. W. Randolph. A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20. J. Pharm. Sci. 91:543-558 (2002).
    • (2002) J. Pharm. Sci. , vol.91 , pp. 543-558
    • Webb, S.D.1    Cleland, J.L.2    Carpenter, J.F.3    Randolph, T.W.4
  • 61
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-γ
    • B. S. Kendrick, J. F. Carpenter, J. L. Cleland, and T. W. Randolph. A transient expansion of the native state precedes aggregation of recombinant human interferon-γ. Proc. Natl. Acad. Sci. USA 95:14142-14146 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 62
    • 0029865430 scopus 로고    scopus 로고
    • Stabilization of recombinant human keratinocyte growth factor by osmolytes and salts
    • B. L. Chen and T. Arakawa. Stabilization of recombinant human keratinocyte growth factor by osmolytes and salts. J. Pharm. Sci. 85:419-422 (1996).
    • (1996) J. Pharm. Sci. , vol.85 , pp. 419-422
    • Chen, B.L.1    Arakawa, T.2
  • 63
    • 0030725266 scopus 로고    scopus 로고
    • Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state
    • B. S. Kendrick, B. S. Chang, T. Arakawa, B. Peterson, T. W. Randolph, M. C. Manning, and J. F. Carpenter. 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 94:11917-11922 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11917-11922
    • Kendrick, B.S.1    Chang, B.S.2    Arakawa, T.3    Peterson, B.4    Randolph, T.W.5    Manning, M.C.6    Carpenter, J.F.7
  • 64
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent-cation salts - Balance between hydration and salt binding
    • T. Arakawa and S. N. Timasheff. Mechanism of protein salting in and salting out by divalent-cation salts - balance between hydration and salt binding. Biochemistry 23:5912-5923 (1984).
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 65
    • 0036784648 scopus 로고    scopus 로고
    • Stabilization of proteins by low molecular weight multi-ions
    • D. S. MacLean, Q. S. Qian, and C. R. Middaugh. Stabilization of proteins by low molecular weight multi-ions. J. Pharm. Sci. 91:2220-2229 (2002).
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2220-2229
    • MacLean, D.S.1    Qian, Q.S.2    Middaugh, C.R.3
  • 66
    • 0035916258 scopus 로고    scopus 로고
    • Effect of salts on the stability and folding of staphylococcal nuclease
    • C. Nishimura, V. N. Uversky, and A. L. Fink. Effect of salts on the stability and folding of staphylococcal nuclease. Biochem. 40:2113-2128 (2001).
    • (2001) Biochem. , vol.40 , pp. 2113-2128
    • Nishimura, C.1    Uversky, V.N.2    Fink, A.L.3
  • 67
    • 0037143801 scopus 로고    scopus 로고
    • Protein-protein interactions in concentrated electrolyte solutions - Hofmeister-series effects
    • R. A. Curtis, J. Ulrich, A. Montaser, J. M. Prausnitz, and H. W. Blanch. Protein-protein interactions in concentrated electrolyte solutions - hofmeister-series effects. Biotechnol. Bioeng. 79:367-380 (2002).
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 367-380
    • Curtis, R.A.1    Ulrich, J.2    Montaser, A.3    Prausnitz, J.M.4    Blanch, H.W.5
  • 68
    • 0026409134 scopus 로고
    • Differential scanning calorimetric studies on bovine serum- albumin. 2. Effects of neutral salts and urea
    • M. Yamasaki, H. Yano, and K. Aoki. Differential scanning calorimetric studies on bovine serum- albumin.2. Effects of neutral salts and urea. Int. J. Biol. Macromol. 13:322-328 (1991).
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 322-328
    • Yamasaki, M.1    Yano, H.2    Aoki, K.3
  • 69
    • 0032822202 scopus 로고    scopus 로고
    • Solubility of recombinant human tissue factor pathway inhibitor
    • B. L. Chen, X. R. Wu, S. J. Babuka, and M. Hora. Solubility of recombinant human tissue factor pathway inhibitor. J. Pharm. Sci. 88:881-888 (1999).
    • (1999) J. Pharm. Sci. , vol.88 , pp. 881-888
    • Chen, B.L.1    Wu, X.R.2    Babuka, S.J.3    Hora, M.4
  • 70
    • 0028895083 scopus 로고
    • A new strategy for enhancing the stability of lyophilized protein - The effect of the reconstitution medium on keratinocyte growth-factor
    • M. Z. Zhang, J. Wen, T. Arakawa, and S. J. Prestrelski. A new strategy for enhancing the stability of lyophilized protein - the effect of the reconstitution medium on keratinocyte growth-factor. Pharm. Res. 12:1447-1452 (1995).
    • (1995) Pharm. Res. , vol.12 , pp. 1447-1452
    • Zhang, M.Z.1    Wen, J.2    Arakawa, T.3    Prestrelski, S.J.4
  • 71
    • 0141474817 scopus 로고    scopus 로고
    • Hydration as a major factor in preferential solvent-protein interactions
    • T. Arakawa. Hydration as a major factor in preferential solvent-protein interactions. Cryst. Growth Des. 2:549-551 (2002).
    • (2002) Cryst. Growth Des. , vol.2 , pp. 549-551
    • Arakawa, T.1
  • 72
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • R. L. Remmele, N. S. Nightlinger, S. Srinivasan, and W. R. Gombotz. Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm. Res. 15:200-208 (1998).
    • (1998) Pharm. Res. , vol.15 , pp. 200-208
    • Remmele, R.L.1    Nightlinger, N.S.2    Srinivasan, S.3    Gombotz, W.R.4
  • 73
    • 0030947271 scopus 로고    scopus 로고
    • Solvent effects on the solubility and physical stability of human insulin-like growth factor I
    • J. Fransson, D. Hallen, and E. FlorinRobertsson. Solvent effects on the solubility and physical stability of human insulin-like growth factor I. Pharm. Res. 14:606-612 (1997).
    • (1997) Pharm. Res. , vol.14 , pp. 606-612
    • Fransson, J.1    Hallen, D.2    FlorinRobertsson, E.3
  • 74
    • 0030990078 scopus 로고    scopus 로고
    • The effect of benzyl alcohol on recombinant human interferon-gamma
    • X. M. Lam, T. W. Patapoff, and T. H. Nguyen. The effect of benzyl alcohol on recombinant human interferon-gamma. Pharm. Res. 14:725-729 (1997).
    • (1997) Pharm. Res. , vol.14 , pp. 725-729
    • Lam, X.M.1    Patapoff, T.W.2    Nguyen, T.H.3
  • 75
    • 0345876459 scopus 로고    scopus 로고
    • Surfactant-stabilized protein formulations: A review of protein-surfactants interactions and novel analytical methodologies
    • Z. Shahrokhs (ed.), American Chemical Society, Washington, DC
    • L. S. Jones, N. B. Bam, and T. W. Randolph. Surfactant-stabilized protein formulations: A review of protein-surfactants interactions and novel analytical methodologies. In Z. Shahrokhs (ed.), Therapeutic Protein and Peptide Formulation and Delivery, American Chemical Society, Washington, DC, 1997, pp. 206-222.
    • (1997) Therapeutic Protein and Peptide Formulation and Delivery , pp. 206-222
    • Jones, L.S.1    Bam, N.B.2    Randolph, T.W.3
  • 76
    • 0031742802 scopus 로고    scopus 로고
    • Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions
    • N. B. Bam, J. L. Cleland, J. Yang, M. C. Manning, J. F. Carpenter, R. F. Kelley, and T. W. Randolph. Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions. J. Pharm. Sci. 87:1554-1559 (1998).
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1554-1559
    • Bam, N.B.1    Cleland, J.L.2    Yang, J.3    Manning, M.C.4    Carpenter, J.F.5    Kelley, R.F.6    Randolph, T.W.7
  • 77
    • 0030292616 scopus 로고    scopus 로고
    • Molten globule intermediate of recombinant human growth hormone: Stabilization with surfactants
    • N. B. Bam, J. L. Cleland, and T. W. Randolph. Molten globule intermediate of recombinant human growth hormone: Stabilization with surfactants. Biotechnol. Prog. 12:801-809 (1996).
    • (1996) Biotechnol. Prog. , vol.12 , pp. 801-809
    • Bam, N.B.1    Cleland, J.L.2    Randolph, T.W.3
  • 79
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins - Intermediates and unfolded states
    • A. L. Fink, L. J. Calciano, Y. Goto, T. Kurotsu, and D. R. Palleros. Classification of acid denaturation of proteins - intermediates and unfolded states. Biochemistry 33:12504-12511 (1994).
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 80
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • R. Carrotta, R. Bauer, R. Waninge, and C. Rischel. Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci. 10:1312-1318 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 82
    • 0031021542 scopus 로고    scopus 로고
    • Conformation of p22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
    • M. A. Speed, T. Morshead, and D. I. C. Wang, and J. King. Conformation of p22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci. 6:99-108 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 99-108
    • Speed, M.A.1    Morshead, T.2    Wang, D.I.C.3    King, J.4
  • 83
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
    • J. King. C. HaasePettingell, A. S. Robinson, M. Speed, and A. Mitraki. Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates. FASEB J. 10:57-66 (1996).
    • (1996) FASEB J. , vol.10 , pp. 57-66
    • King, J.1    HaasePettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 84
    • 0030582355 scopus 로고    scopus 로고
    • Folding pathway of human alpha(1)-antitrypsin: Characterization of an intermediate that is active but prone to aggregation
    • D. Y. Kim and M. H. Yu. Folding pathway of human alpha(1)-antitrypsin: Characterization of an intermediate that is active but prone to aggregation. Biochem. Biophys. Res. Commun. 226:378-384 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 378-384
    • Kim, D.Y.1    Yu, M.H.2
  • 85
  • 87
    • 0035912726 scopus 로고    scopus 로고
    • Partial molar volume, surface area, hydration changes for equilibrium unfolding and formation of aggregation transition state: High-pressure and cosolute studies on recombinant human ifn-γ
    • J. N. Webb, S. D. Webb, J. L. Cleland, J. F. Carpenter, and T. W. Randolph. Partial molar volume, surface area, hydration changes for equilibrium unfolding and formation of aggregation transition state: High-pressure and cosolute studies on recombinant human ifn-γ. Proc. Natl. Acad. Sci. USA 98:7259-7264 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7259-7264
    • Webb, J.N.1    Webb, S.D.2    Cleland, J.L.3    Carpenter, J.F.4    Randolph, T.W.5
  • 88
    • 0028308524 scopus 로고
    • Time-resolved resonance raman-spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin
    • J. M. Friedman. Time-resolved resonance raman-spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin. Methods Enzymol. 232:205-231 (1994).
    • (1994) Methods Enzymol. , vol.232 , pp. 205-231
    • Friedman, J.M.1
  • 89
    • 84990475356 scopus 로고
    • Structure dynamics of proteins by hydrogen-exchange methods
    • A. D. Barksdale, D. G. Knox, and A. Rosenberg. Structure dynamics of proteins by hydrogen-exchange methods. Biophys. J. 32:619-621 (1980).
    • (1980) Biophys. J. , vol.32 , pp. 619-621
    • Barksdale, A.D.1    Knox, D.G.2    Rosenberg, A.3
  • 90
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • J. M. Sanchez-Ruiz. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophy. J. 61:921-935 (1992).
    • (1992) Biophy. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 91
    • 0020814787 scopus 로고
    • On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes
    • S. E. Zale and A. M. Klibanov. On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes. Biotechnol. Bioeng. 25:2221-2230 (1983).
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 2221-2230
    • Zale, S.E.1    Klibanov, A.M.2
  • 92
    • 0024037737 scopus 로고
    • Mechanism of protein precipitation and stabilization by co-solvents
    • S. N. Timasheff and T. Arakawa. Mechanism of protein precipitation and stabilization by co-solvents. J. Cryst. Growth 90:39-46 (1988).
    • (1988) J. Cryst. Growth , vol.90 , pp. 39-46
    • Timasheff, S.N.1    Arakawa, T.2
  • 94
    • 5844235959 scopus 로고    scopus 로고
    • Phase behavior of small attractive colloidal particles
    • D. Rosenbaum, P. C. Zamora, and C. F. Zukoski. Phase behavior of small attractive colloidal particles. Phys. Rev. Lett. 76:150-153 (1996).
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 150-153
    • Rosenbaum, D.1    Zamora, P.C.2    Zukoski, C.F.3
  • 95
    • 0033513680 scopus 로고    scopus 로고
    • Understanding protein crystallization on the basis of the phase diagram
    • C. Haas and J. Drenth. Understanding protein crystallization on the basis of the phase diagram. J. Cryst. Growth 196:388-394 (1999).
    • (1999) J. Cryst. Growth , vol.196 , pp. 388-394
    • Haas, C.1    Drenth, J.2
  • 96
    • 0035967401 scopus 로고    scopus 로고
    • Calculation of phase diagrams for aqueous protein solutions
    • R. A. Curtis, H. W. Blanch, and J. M. Prausnitz. Calculation of phase diagrams for aqueous protein solutions. J. Phys. Chem. B 105:2445-2452 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2445-2452
    • Curtis, R.A.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 97
    • 0033033595 scopus 로고    scopus 로고
    • Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor
    • M. Farnum and C. Zukoski. Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor. Biophys. J. 76:2716-2726 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 2716-2726
    • Farnum, M.1    Zukoski, C.2
  • 98
    • 0033513739 scopus 로고    scopus 로고
    • Correlation of second virial coefficients and solubilities useful in protein crystal growth
    • B. Guo, S. Kao, H. McDonald, A. Asanov, L. L. Combs, and W. W. Wilson. Correlation of second virial coefficients and solubilities useful in protein crystal growth. J. Cryst. Growth 196:424-433 (1999).
    • (1999) J. Cryst. Growth , vol.196 , pp. 424-433
    • Guo, B.1    Kao, S.2    McDonald, H.3    Asanov, A.4    Combs, L.L.5    Wilson, W.W.6
  • 99
    • 0001516764 scopus 로고    scopus 로고
    • Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution
    • C. Haas, J. Drenth, and W. W. Wilson. Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution. J. Phys. Chem. B 103:2808-2811 (1999).
    • (1999) J. Phys. Chem. B , vol.103 , pp. 2808-2811
    • Haas, C.1    Drenth, J.2    Wilson, W.W.3
  • 100
    • 0030566439 scopus 로고    scopus 로고
    • Protein interactions and crystallization
    • D. F. Rosenbaum and C. F. Zukoski. Protein interactions and crystallization. J. Cryst. Growth 169:752-758 (1996).
    • (1996) J. Cryst. Growth , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 101
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • A. George and W. W. Wilson. Predicting protein crystallization from a dilute solution property. Acta Cryst. D50:361-365 (1994).
    • (1994) Acta Cryst. , vol.D50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 102
    • 0034616954 scopus 로고    scopus 로고
    • Protein crystallization by desigh: Chymotrypsinogen without precipitants
    • P. E. Pjura, A. M. Lenhoff, S. A. Leonard, and A. G. Gittis. Protein crystallization by desigh: Chymotrypsinogen without precipitants. J. Mol. Biol. 300:235-239 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 235-239
    • Pjura, P.E.1    Lenhoff, A.M.2    Leonard, S.A.3    Gittis, A.G.4
  • 103
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • O. D. Velev, E. W. Kaler, and A. M. Lenhoff. Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys. J. 75:2682-2697 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 105
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea
    • D. Hamada and C. M. Dobson. A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11:2417-2426 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 106
    • 0027270578 scopus 로고
    • A kinetic-model for amyloid formation in the prion diseases - Importance of seeding
    • J. H. Come, P. E. Fraser, and P. T. Lansbury. A kinetic-model for amyloid formation in the prion diseases - importance of seeding. Proc. Natl. Acad. Sci. USA 90:5959-5963 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 107
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an sh 3 domain
    • J. Zurdo, J. I. Guijarro, J. L. Jimenez, H. R. Saibil, and C. M. Dobson. Dependence on solution conditions of aggregation and amyloid formation by an sh3 domain. J. Mol. Biol. 311:325-340 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.I.2    Jimenez, J.L.3    Saibil, H.R.4    Dobson, C.M.5
  • 108
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • S. M. Chen, V. Berthelier, J. B. Hamilton, B. O'Nuallain, and R. Wetzel. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochem. 41:7391-7399 (2002).
    • (2002) Biochem. , vol.41 , pp. 7391-7399
    • Chen, S.M.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 111
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • H. Naiki and F. Gejyo. Kinetic analysis of amyloid fibril formation. Methods Enzymol. 309:305-318 (1999).
    • (1999) Methods Enzymol. , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.