메뉴 건너뛰기




Volumn 14, Issue 9, 2005, Pages 2258-2266

High-pressure studies of aggregation of recombinant human interleukin-1 receptor antagonist: Thermodynamics, kinetics, and application to accelerated formulation studies

Author keywords

Coefficient of adiabatic compressibility; Disulfide bonds; Protein structure folding; Specific volume

Indexed keywords

CYSTEINE; RECOMBINANT INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; RECOMBINANT PROTEIN; SOLVENT;

EID: 24344491042     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051490205     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 0037825776 scopus 로고    scopus 로고
    • Exploring the entire conformational space of proteins by high-pressure NMR
    • Akasaka, K. 2003. Exploring the entire conformational space of proteins by high-pressure NMR. Pure Appl. Chem. 75: 927-936.
    • (2003) Pure Appl. Chem. , vol.75 , pp. 927-936
    • Akasaka, K.1
  • 3
    • 27744467601 scopus 로고
    • Activation and reaction volumes in solution
    • Asano, T. and Lenoble, J. 1978. Activation and reaction volumes in solution. Chem. Rev. 78: 407-489.
    • (1978) Chem. Rev. , vol.78 , pp. 407-489
    • Asano, T.1    Lenoble, J.2
  • 4
    • 0012223420 scopus 로고    scopus 로고
    • High pressure and protein oligomeric dissociation
    • Balny, C. 2002. High pressure and protein oligomeric dissociation. High Pressure Res. 22: 737-741.
    • (2002) High Pressure Res. , vol.22 , pp. 737-741
    • Balny, C.1
  • 5
    • 0002203625 scopus 로고    scopus 로고
    • Early stages of protein folding
    • ed. R.H. Pain Oxford University Press, Oxford, UK
    • Bierri, O. and Kiefhaber, T. 2000. Early stages of protein folding. In Mechanisms of protein folding (ed. R.H. Pain), pp. 34-64. Oxford University Press, Oxford, UK.
    • (2000) Mechanisms of Protein Folding , pp. 34-64
    • Bierri, O.1    Kiefhaber, T.2
  • 6
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation - Effect of pressure on denaturation of ribonuclease-A
    • Brandts, J.F., Oliveira, R.J., and Westort, C. 1970. Thermodynamics of protein denaturation - Effect of pressure on denaturation of ribonuclease-A. Biochemistry 9: 1038-1047.
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brandts, J.F.1    Oliveira, R.J.2    Westort, C.3
  • 7
    • 0037946173 scopus 로고    scopus 로고
    • Influence of pressure on chemical equilibria in aqueous systems - With particular reference to seawater
    • Byrne, R.H. and Laurie, S.H. 1999. Influence of pressure on chemical equilibria in aqueous systems - With particular reference to seawater. Pure Appl. Chem. 71: 871-890.
    • (1999) Pure Appl. Chem. , vol.71 , pp. 871-890
    • Byrne, R.H.1    Laurie, S.H.2
  • 8
    • 84957958139 scopus 로고
    • Oxidation of thiols
    • ed. S. Patai John Wiley & Sons, New York
    • Capozzi, G. and Modena, G. 1974. Oxidation of thiols. In The chemistry of the thiol group (ed. S. Patai), pp. 785-840. John Wiley & Sons, New York.
    • (1974) The Chemistry of the Thiol Group , pp. 785-840
    • Capozzi, G.1    Modena, G.2
  • 9
    • 0029751965 scopus 로고    scopus 로고
    • Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution
    • Chang, B.S., Beauvais, R.M., Arakawa, T., Narhi, L.O., Dong, A.C., Aparisio, D.I., and Carpenter, J.F. 1996. Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution. Biophys. J. 71: 3399-3406.
    • (1996) Biophys. J. , vol.71 , pp. 3399-3406
    • Chang, B.S.1    Beauvais, R.M.2    Arakawa, T.3    Narhi, L.O.4    Dong, A.C.5    Aparisio, D.I.6    Carpenter, J.F.7
  • 10
    • 0037046166 scopus 로고    scopus 로고
    • Comparison of heat- and pressure-induced unfolding of ribonuclease A: The critical role of Phe46 which appears to belong to a new hydrophobic chain-folding initiation site
    • Chatani, E., Nonomura, K., Hayashi, R., Balny, C., and Lange, R. 2002. Comparison of heat- and pressure-induced unfolding of ribonuclease A: The critical role of Phe46 which appears to belong to a new hydrophobic chain-folding initiation site. Biochemistry 41: 4567-4574.
    • (2002) Biochemistry , vol.41 , pp. 4567-4574
    • Chatani, E.1    Nonomura, K.2    Hayashi, R.3    Balny, C.4    Lange, R.5
  • 11
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E.Y., Krishnan, S., Randolph, T.W., and Carpenter, J.F. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20: 1325-1336.
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 12
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • Clark, E.D. 2001. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 12: 202-207.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 202-207
    • Clark, E.D.1
  • 13
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-I infrared-spectra
    • Dong, A., Huang, P., and Caughey, W.S. 1990. Protein secondary structures in water from 2nd-derivative amide-I infrared-spectra. Biochemistry 29: 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 17
    • 0022999267 scopus 로고
    • Compressibility structure relationship of globular-proteins
    • Gekko, K. and Hasegawa, Y. 1986. Compressibility structure relationship of globular-proteins. Biochemistry 25: 6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 18
    • 0000092070 scopus 로고
    • Effect of temperature on the compressibility of native globular-proteins
    • _. 1989. Effect of temperature on the compressibility of native globular-proteins. J. Phys. Chem. 93: 426-429.
    • (1989) J. Phys. Chem. , vol.93 , pp. 426-429
  • 19
    • 0028220701 scopus 로고
    • Proteins under pressure - The influence of high hydrostatic-pressure on structure, function and assembly of proteins and protein complexes
    • Gross, M. and Jaenicke, R. 1994. Proteins under pressure - The influence of high hydrostatic-pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221: 617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 20
    • 0002155704 scopus 로고
    • The role of electrostriction in high-pressure chemistry
    • Hamann, S.D. 1980. The role of electrostriction in high-pressure chemistry. Review of Physical Chemistry of Japan 50: 147-168.
    • (1980) Review of Physical Chemistry of Japan , vol.50 , pp. 147-168
    • Hamann, S.D.1
  • 21
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley, S.A. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10: 2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 22
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 23
    • 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
    • Kendrick, B.S., Chang, B.S., Arakawa, T., Peterson, B., Randolph, T.W., Manning, M.C., and Carpenter, J.F. 1997. Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state. Proc. Natl. Acad. Sci. 94: 11917-11922.
    • (1997) Proc. Natl. Acad. Sci. , 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
  • 25
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein - Insights into transition states from pressure, temperature, and co-solute studies
    • Kim, Y.S., Randolph, T.W., Stevens, F.J., and Carpenter, J.F. 2002. Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein - Insights into transition states from pressure, temperature, and co-solute studies. J. Biol. Chem. 277: 27240-27246.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27240-27246
    • Kim, Y.S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 26
    • 20144365303 scopus 로고    scopus 로고
    • Protein phase diagrams: The physics behind their elliptic shape
    • Lesch, H., Hecht, C., and Friedrich, J. 2004. Protein phase diagrams: The physics behind their elliptic shape. J. Chem. Phys. 121: 12671-12675.
    • (2004) J. Chem. Phys. , vol.121 , pp. 12671-12675
    • Lesch, H.1    Hecht, C.2    Friedrich, J.3
  • 27
    • 0008823209 scopus 로고    scopus 로고
    • Pressure-assisted cold unfolding of proteins and its effects on the conformational stability compared to pressure and heat unfolding
    • Meersman, F., Smeller, L., and Heremans, K. 2000. Pressure-assisted cold unfolding of proteins and its effects on the conformational stability compared to pressure and heat unfolding. High Pressure Res. 19: 653-658.
    • (2000) High Pressure Res. , vol.19 , pp. 653-658
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 28
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • _. 2002. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82: 2635-2644.
    • (2002) Biophys. J. , vol.82 , pp. 2635-2644
  • 29
    • 0030065265 scopus 로고    scopus 로고
    • High pressure effects on protein structure and function
    • Mozhaev, V.V., Heremans, K., Frank, J., Masson, P., and Balny, C. 1996. High pressure effects on protein structure and function. Proteins 24: 81-91.
    • (1996) Proteins , vol.24 , pp. 81-91
    • Mozhaev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 30
    • 0346850625 scopus 로고    scopus 로고
    • Volumetric characterization of homopolymeric amino acids
    • Noudeh, G.D., Taulier, N., and Chalikian, T.V. 2003. Volumetric characterization of homopolymeric amino acids. Biopolymers 70: 563-574.
    • (2003) Biopolymers , vol.70 , pp. 563-574
    • Noudeh, G.D.1    Taulier, N.2    Chalikian, T.V.3
  • 31
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Pace, C.N. and Shaw, K.L. 2000. Linear extrapolation method of analyzing solvent denaturation curves. Proteins (Suppl. 4): 1-7.
    • (2000) Proteins , Issue.4 SUPPL. , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 33
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by 2nd-derivative spectroscopy
    • Ragone, R., Colonna, G., Balestrieri, C., Servillo, L., and Irace, G. 1984. Determination of tyrosine exposure in proteins by 2nd-derivative spectroscopy. Biochemistry 23: 1871-1875.
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 34
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life
    • Roberts, C.J. 2003. Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life. J. Phys. Chem. B 107: 1194-1207.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1194-1207
    • Roberts, C.J.1
  • 35
    • 0242684664 scopus 로고    scopus 로고
    • Irreversible aggregation of recombinant bovine Granulocyte-Colony Stimulating Factor (bG-CSF) and implications for predicting protein shelf life
    • Roberts, C.J., Darrington, R.T., and Whitley, M.B. 2003. Irreversible aggregation of recombinant bovine Granulocyte-Colony Stimulating Factor (bG-CSF) and implications for predicting protein shelf life. J. Pharm. Sci. 92: 1095-1111.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 1095-1111
    • Roberts, C.J.1    Darrington, R.T.2    Whitley, M.B.3
  • 36
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer, C.A. 2002. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595: 201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 37
    • 0037171142 scopus 로고    scopus 로고
    • High pressure static fluorescence to study macromolecular structure-function
    • Ruan, K. and Balny, C. 2002. High pressure static fluorescence to study macromolecular structure-function. Biochim. Biophys. Acta 1595: 94-102.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 94-102
    • Ruan, K.1    Balny, C.2
  • 38
    • 0032813545 scopus 로고    scopus 로고
    • Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution
    • Sasahara, K. and Nitta, K. 1999. Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution. Protein Sci. 8: 1469-1474.
    • (1999) Protein Sci. , vol.8 , pp. 1469-1474
    • Sasahara, K.1    Nitta, K.2
  • 39
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley, M.L. and Baker, D. 1997. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc. Natl. Acad. Sci. 94: 10636-10640.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 43
    • 0033539596 scopus 로고    scopus 로고
    • High pressure fosters protein refolding from aggregates at high concentrations
    • St. John, R.J., Carpenter, J.F., and Randolph, T.W. 1999. High pressure fosters protein refolding from aggregates at high concentrations. Proc. Natl. Acad. Sci. 96: 13029-13033.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 13029-13033
    • St. John, R.J.1    Carpenter, J.F.2    Randolph, T.W.3
  • 45
    • 0030940855 scopus 로고    scopus 로고
    • Site-specific modification of rabbit muscle creatine kinase with sulfhydryl-specific fluorescence probe by use of hydrostatic pressure
    • Tanaka, N., Tonai, T., and Kunugi, S. 1997. Site-specific modification of rabbit muscle creatine kinase with sulfhydryl-specific fluorescence probe by use of hydrostatic pressure. Biochim. Biophys. Acta 1339: 226-232.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 226-232
    • Tanaka, N.1    Tonai, T.2    Kunugi, S.3
  • 46
    • 0035918582 scopus 로고    scopus 로고
    • Pressure-induced perturbation on the active site of β-amylase monitored from the sulfhydryl reaction
    • Tanaka, N., Mitani, D., and Kunugi, S. 2001. Pressure-induced perturbation on the active site of β-amylase monitored from the sulfhydryl reaction. Biochemistry 40: 5914-5920.
    • (2001) Biochemistry , vol.40 , pp. 5914-5920
    • Tanaka, N.1    Mitani, D.2    Kunugi, S.3
  • 47
  • 49
    • 0035913512 scopus 로고    scopus 로고
    • A model for studying drying at hydrophobic interfaces: Structural and thermodynamic properties
    • Wallqvist, A., Gallicchio, E., and Levy, R.M. 2001. A model for studying drying at hydrophobic interfaces: Structural and thermodynamic properties. J. Phys. Chem. B 105: 6745-6753.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6745-6753
    • Wallqvist, A.1    Gallicchio, E.2    Levy, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.