메뉴 건너뛰기




Volumn 12, Issue 5, 2003, Pages 903-913

Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor

Author keywords

Activation energy; Light scattering; Non native protein aggregation; Osmotic second virial coefficient; Protein formulation strategy; Protein interactions; Protein stability; RhGCSF

Indexed keywords

RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR;

EID: 0242515822     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0235703     Document Type: Article
Times cited : (304)

References (43)
  • 1
    • 0003516749 scopus 로고
    • W.H. Freeman and Company, New York
    • Atkins, P. 1994. Physical chemistry, 5th ed., p. 1031. W.H. Freeman and Company, New York.
    • (1994) Physical Chemistry, 5th Ed. , pp. 1031
    • Atkins, P.1
  • 3
    • 0034308128 scopus 로고    scopus 로고
    • Measured and calculated effects of mutations in bacteriophage T4 lysozyme on interactions in solution
    • Chang, R.C., Asthagiri, D., and Lenhoff, A.M. 2000. Measured and calculated effects of mutations in bacteriophage T4 lysozyme on interactions in solution. Proteins 41: 123-132.
    • (2000) Proteins , vol.41 , pp. 123-132
    • Chang, R.C.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 4
    • 0034327347 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared and circular dichroism spectroscopic analysis of α(1)-proteinase inhibitor and ovalbumin in aqueous solution
    • Dong, A.C., Meyer, J.D., Brown, J.L., Manning, M.C., and Carpenter, J.F. 2000. Comparative Fourier transform infrared and circular dichroism spectroscopic analysis of α(1)-proteinase inhibitor and ovalbumin in aqueous solution. Arch. Biochem. Biophys. 383: 148-155.
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 148-155
    • Dong, A.C.1    Meyer, J.D.2    Brown, J.L.3    Manning, M.C.4    Carpenter, J.F.5
  • 5
    • 0033033595 scopus 로고    scopus 로고
    • Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor
    • Farnum, M. and Zukoski, C. 1999. Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor. Biophys. J. 76: 2716-2726.
    • (1999) Biophys. J. , vol.76 , pp. 2716-2726
    • Farnum, M.1    Zukoski, C.2
  • 6
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Design 3: R9-R23.
    • (1998) Fold Design , vol.3
    • Fink, A.L.1
  • 7
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George, A. and Wilson, W.W. 1994. Predicting protein crystallization from a dilute solution property. Acta Crystallogr. D50: 361-365.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 9
    • 0033513739 scopus 로고    scopus 로고
    • Correlation of second virial coefficients and solubilities useful in protein crystal growth
    • Guo, B., Kao, S., McDonald, H., Asanov, A., Combs, L.L., and Wilson, W.W. 1999. Correlation of second virial coefficients and solubilities useful in protein crystal growth. J. Crystallogr. Growth 196: 424-433.
    • (1999) J. Crystallogr. 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
  • 10
    • 0033513680 scopus 로고    scopus 로고
    • Understanding protein crystallization on the basis of the phase diagram
    • Haas, C. and Drenth, J. 1999. Understanding protein crystallization on the basis of the phase diagram. J. Crystallogr. Growth 196: 388-394.
    • (1999) J. Crystallogr. Growth , vol.196 , pp. 388-394
    • Haas, C.1    Drenth, J.2
  • 11
    • 0001516764 scopus 로고    scopus 로고
    • Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution
    • Haas, C., Drenth, J., and Wilson, W.W. 1999. 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) J. Phys. Chem. B , vol.103 , pp. 2808-2811
    • Haas, C.1    Drenth, J.2    Wilson, W.W.3
  • 13
    • 0027258762 scopus 로고
    • The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors
    • Hill, C.P., Osslund, T.D., and Eisenberg, D. 1993. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. 90: 5167-5171.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 15
    • 0030052290 scopus 로고    scopus 로고
    • Role of hydration and water structure in biological and colloidal interactions
    • Israelachvili, J. and Wennerström, H. 1996. Role of hydration and water structure in biological and colloidal interactions. Nature 379: 219-225.
    • (1996) Nature , vol.379 , pp. 219-225
    • Israelachvili, J.1    Wennerström, H.2
  • 16
    • 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
  • 17
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-g
    • Kendrick, B.S., Carpenter, J.F., Cleland, J.L., and Randolph, T.W. 1998. A transient expansion of the native state precedes aggregation of recombinant human interferon-g. Proc. Natl. Acad. Sci. 95: 14142-14146.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 18
    • 0035894420 scopus 로고    scopus 로고
    • Online size-exclusion high-performance liquid chromatograpy light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states
    • Kendrick, B.S., Kerwin, B.A., Chang, B.S., and Philo, J.S. 2001. Online size-exclusion high-performance liquid chromatograpy light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states. Anal. Biochem. 299: 136-146.
    • (2001) Anal. Biochem. , vol.299 , pp. 136-146
    • Kendrick, B.S.1    Kerwin, B.A.2    Chang, B.S.3    Philo, J.S.4
  • 20
    • 0030774543 scopus 로고    scopus 로고
    • Granulocyte-colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH 2
    • Kolvenbach, C.G., Narhi, L.O., Philo, J.S., Li, T., Zhang, M., and Arakawa, T. 1997. Granulocyte-colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH 2. J. Peptide Res. 50: 310-318.
    • (1997) J. Peptide Res. , vol.50 , pp. 310-318
    • Kolvenbach, C.G.1    Narhi, L.O.2    Philo, J.S.3    Li, T.4    Zhang, M.5    Arakawa, T.6
  • 21
    • 0037150072 scopus 로고    scopus 로고
    • Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition
    • Krishnan, S., Chi, E.Y., Webb, J.N., Chang, B.S., Shan, D., Goldenberg, M., Manning, M.C., Randolph, T.W., and Carpenter, J.F. 2002. Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition. Biochemistry 41: 6422-6431.
    • (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
  • 22
    • 0036228118 scopus 로고    scopus 로고
    • Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein
    • Lee, K.K., Fitch, C.A., and Garcia-Moreno, B. 2002. Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein. Protein Sci. 11: 1004-1016.
    • (2002) Protein Sci. , vol.11 , pp. 1004-1016
    • Lee, K.K.1    Fitch, C.A.2    Garcia-Moreno, B.3
  • 24
    • 0033080174 scopus 로고    scopus 로고
    • Chemical modification and site-directed mutagenesis of methionine residues in recombinant human granulocyte colony stimulating factor: Effect on stability and biological activity
    • Lu, H.S., Fausset, P.R., Narhi, L.O., Horan, T., Shinagawa, K., Shimamoto, G., and Boone, T. 1999. Chemical modification and site-directed mutagenesis of methionine residues in recombinant human granulocyte colony stimulating factor: effect on stability and biological activity. Arch. Biochem. Biophys. 362: 1-11.
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 1-11
    • Lu, H.S.1    Fausset, P.R.2    Narhi, L.O.3    Horan, T.4    Shinagawa, K.5    Shimamoto, G.6    Boone, T.7
  • 25
  • 27
    • 0025734440 scopus 로고
    • Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride
    • Narhi, L.O., Kenney, W.C., and Arakawa, T. 1991. Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride. J. Protein Chem. 10: 359-367.
    • (1991) J. Protein Chem. , vol.10 , pp. 359-367
    • Narhi, L.O.1    Kenney, W.C.2    Arakawa, T.3
  • 28
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • Neal, B.L., Asthagiri, D., and Lenhoff, A. 1998. Molecular origins of osmotic second virial coefficients of proteins. Biophys. J. 75: 2469-2477.
    • (1998) Biophys. J. , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.3
  • 29
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131: 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 30
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • -. 1990. Measuring and increasing protein stability. Trends Biotechnol. 8: 93-98.
    • (1990) Trends Biotechnol , vol.8 , pp. 93-98
  • 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 4: 1-7.
    • (2000) Proteins , vol.4 , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 32
    • 0000650211 scopus 로고
    • Diffusion of charged colloidal particles at low volume fraction: Theoretical model and light scattering measurements
    • Petsev, D.N. and Denkov, N.D. 1992. Diffusion of charged colloidal particles at low volume fraction: Theoretical model and light scattering measurements. J. Colloid Interface Sci. 149: 329-344.
    • (1992) J. Colloid Interface Sci. , vol.149 , pp. 329-344
    • Petsev, D.N.1    Denkov, N.D.2
  • 33
    • 0034082815 scopus 로고    scopus 로고
    • Interactions and aggregation of apoferritin molecules in solution: Effects of added electrolytes
    • Petsev, D.N., Thomas, B.R., Yau, S.T., and Vekilov, P.G. 2000. Interactions and aggregation of apoferritin molecules in solution: Effects of added electrolytes. Biophys. J. 78: 2060-2069.
    • (2000) Biophys. J. , vol.78 , pp. 2060-2069
    • Petsev, D.N.1    Thomas, B.R.2    Yau, S.T.3    Vekilov, P.G.4
  • 34
    • 0034616954 scopus 로고    scopus 로고
    • Protein crystallization by design: Chymotrypsinogen without precipitants
    • Pjura, P.E., Lenhoff, A.M., Leonard, S.A., and Gittis, A.G. 2000. Protein crystallization by design: Chymotrypsinogen without precipitants. J. Mol. Biol. 300: 235-239.
    • (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
  • 35
    • 5844235959 scopus 로고    scopus 로고
    • Phase behavior of small attractive colloidal particles
    • Rosenbaum, D., Zamora, P.C., and Zukoski, C.F. 1996. Phase behavior of small attractive colloidal particles. Phys. Rev. Lett. 76: 150-153.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 150-153
    • Rosenbaum, D.1    Zamora, P.C.2    Zukoski, C.F.3
  • 36
    • 0042440398 scopus 로고    scopus 로고
    • Protein interactions and phase behavior: Sensitivity to the form of the pair potential
    • Rosenbaum, D.F., Kulkarni, A., Ramakrishnan, S., and Zukoski, C.F. 1999. Protein interactions and phase behavior: Sensitivity to the form of the pair potential. J. Chem. Phys. 111: 9882-9890.
    • (1999) J. Chem. Phys. , vol.111 , pp. 9882-9890
    • Rosenbaum, D.F.1    Kulkarni, A.2    Ramakrishnan, S.3    Zukoski, C.F.4
  • 37
    • 0035823222 scopus 로고    scopus 로고
    • Protein refolding versus aggregation: Computer simulation on an intermediate-resolution protein model
    • Smith, A.V. and Hall, C.K. 2001. Protein refolding versus aggregation: Computer simulation on an intermediate-resolution protein model. J. Mol. Biol. 312: 187-202.
    • (2001) J. Mol. Biol. , vol.312 , pp. 187-202
    • Smith, A.V.1    Hall, C.K.2
  • 38
    • 0029108966 scopus 로고
    • Use of glycerol, polyols, and other protein structure stabilizing agents in protein crystallization
    • Sousa, R. 1995. Use of glycerol, polyols, and other protein structure stabilizing agents in protein crystallization. Acta Crystallogr. D51: 271-277.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 271-277
    • Sousa, R.1
  • 39
  • 42
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev, O.D., Kaler, E.W., and Lenhoff, A.M. 1998. Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys. J. 75: 2682-2697.
    • (1998) Biophys. J. , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 43
    • 0035912726 scopus 로고    scopus 로고
    • Partial molar volume, surface area, hydration changes for equilibrium unfolding and formation of aggregation transition state: Pressure and cosolute studies on recombinant human IFN-g
    • Webb, J.N., Webb, S.D., Cleland, J.L., Carpenter, J.F., and Randolph, T.W. 2001. Partial molar volume, surface area, hydration changes for equilibrium unfolding and formation of aggregation transition state: pressure and cosolute studies on recombinant human IFN-g. Proc. Natl. Acad. Sci. 98: 7259-7264.
    • (2001) Proc. Natl. Acad. Sci. , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.