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Volumn 486, Issue 1-2, 2015, Pages 131-135

Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins

Author keywords

Aggregation; Calorimetry; DSC; Formulation; Osmolyte; Stabilization

Indexed keywords

ARGININE; BOVINE SERUM ALBUMIN; GLOBULAR PROTEIN; GLYCINE; GUANIDINE; MYOGLOBIN;

EID: 84963978439     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2015.03.051     Document Type: Article
Times cited : (51)

References (32)
  • 1
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • T. Arakawa, and S. Timasheff Preferential interactions of proteins with solvent components in aqueous amino acid solutions Archiv. Biochem. Biophys. 224 1983 169 177
    • (1983) Archiv. Biochem. Biophys. , vol.224 , pp. 169-177
    • Arakawa, T.1    Timasheff, S.2
  • 2
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • T. Arakawa, and K. Tsumoto The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation Biochem. Biophys. Res. Commun. 304 2003 148 152
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 3
    • 35448968555 scopus 로고    scopus 로고
    • Biotechnology applications of amino acids in protein purification and formulations
    • T. Arakawa, K. Tsumoto, Y. Kita, B. Chang, and D. Ejima Biotechnology applications of amino acids in protein purification and formulations Amino Acids 33 2007 587 605
    • (2007) Amino Acids , vol.33 , pp. 587-605
    • Arakawa, T.1    Tsumoto, K.2    Kita, Y.3    Chang, B.4    Ejima, D.5
  • 4
    • 84885145262 scopus 로고    scopus 로고
    • Influence of osmolytes on protein and water structure: A step to understanding the mechanism of protein stabilization
    • P. Bruździak, A. Panuszko, and J. Stangret Influence of osmolytes on protein and water structure: a step to understanding the mechanism of protein stabilization J. Phys. Chem. B 117 2013 11502 11508
    • (2013) J. Phys. Chem. B , vol.117 , pp. 11502-11508
    • Bruździak, P.1    Panuszko, A.2    Stangret, J.3
  • 5
    • 84892571753 scopus 로고    scopus 로고
    • Thermal stability of lysozyme as a function of ion concentration: A reappraisal of the relationship between the Hofmeister series and protein stability
    • J.W. Bye, and R.J. Falconer Thermal stability of lysozyme as a function of ion concentration: A reappraisal of the relationship between the Hofmeister series and protein stability Prot. Sci. 22 2013 1563 1570
    • (2013) Prot. Sci. , vol.22 , pp. 1563-1570
    • Bye, J.W.1    Falconer, R.J.2
  • 6
    • 84899489971 scopus 로고    scopus 로고
    • Three stages of lysozyme thermal stabilization by high and medium charge density anions
    • J.W. Bye, and R.J. Falconer Three stages of lysozyme thermal stabilization by high and medium charge density anions J. Phys. Chem. B 118 2014 4282 4286
    • (2014) J. Phys. Chem. B , vol.118 , pp. 4282-4286
    • Bye, J.W.1    Falconer, R.J.2
  • 7
    • 84898548894 scopus 로고    scopus 로고
    • Biopharmaceutical liquid formulation: A review of the science of protein stability and solubility in aqueous environments
    • J.W. Bye, L. Platts, and R.J. Falconer Biopharmaceutical liquid formulation: a review of the science of protein stability and solubility in aqueous environments Biotechnol. Lett. 36 2014 869 875
    • (2014) Biotechnol. Lett. , vol.36 , pp. 869-875
    • Bye, J.W.1    Platts, L.2    Falconer, R.J.3
  • 9
    • 0035176391 scopus 로고    scopus 로고
    • Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein processes and changes in water-accessible surface area
    • E.S. Courtenay, M.W. Capp, and M.T. Record Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area Prot. Sci. 10 2001 2485 2497
    • (2001) Prot. Sci. , vol.10 , pp. 2485-2497
    • Courtenay, E.S.1    Capp, M.W.2    Record, M.T.3
  • 10
    • 43149117084 scopus 로고    scopus 로고
    • Inhibition of protein aggregation: Supramolecular assemblies of arginine hold the key
    • U. Das, G. Hariprasad, and A.S. Ethayathulla Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key PLoS One 2 2007 e1176
    • (2007) PLoS One , vol.2 , pp. e1176
    • Das, U.1    Hariprasad, G.2    Ethayathulla, A.S.3
  • 11
    • 79958742888 scopus 로고    scopus 로고
    • Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients
    • R.J. Falconer, C. Chan, K. Hughes, and T.P. Munro Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients J. Chem. Technol. Biotechnol. 86 2011 942 948
    • (2011) J. Chem. Technol. Biotechnol. , vol.86 , pp. 942-948
    • Falconer, R.J.1    Chan, C.2    Hughes, K.3    Munro, T.P.4
  • 12
    • 0016292941 scopus 로고
    • Urea and guanidinium hydrogenchloirde denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • R.F. Greene, and C.N. Pace Urea and guanidinium hydrogenchloirde denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin J. Biol. Chem. 249 1974 5388 5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 15
    • 0028618410 scopus 로고
    • Contribution of the surface free energy perturbation to protein-solvent interactions
    • Y. Kita, T. Arakawa, T.Y. Lin, and S.N. Timasheff Contribution of the surface free energy perturbation to protein-solvent interactions Biochemistry 33 1994 15178 15189
    • (1994) Biochemistry , vol.33 , pp. 15178-15189
    • Kita, Y.1    Arakawa, T.2    Lin, T.Y.3    Timasheff, S.N.4
  • 16
    • 0015950174 scopus 로고
    • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
    • J.C. Lee, and S.N. Timasheff Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride Biochemistry 13 1974 257 265
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, J.C.1    Timasheff, S.N.2
  • 17
    • 62449341938 scopus 로고    scopus 로고
    • Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
    • W.K. Lim, J. Rösgen, and S.W. Englander Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group Proc. Natl. Acad. Sci. U. S. A. 106 2009 2595 2600
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2595-2600
    • Lim, W.K.1    Rösgen, J.2    Englander, S.W.3
  • 18
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Y. Liu, and D.W. Bolen The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes Biochemistry 34 1995 12884 12891
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 19
    • 9644310200 scopus 로고    scopus 로고
    • Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains
    • A. Möglich, F. Krieger, and T. Kiefhaber Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains J. Mol. Biol. 345 2005 153 162
    • (2005) J. Mol. Biol. , vol.345 , pp. 153-162
    • Möglich, A.1    Krieger, F.2    Kiefhaber, T.3
  • 20
    • 0034176272 scopus 로고    scopus 로고
    • The formulation of biopharmaceutical products
    • D.A. Parkins, and U.T. Lashmar The formulation of biopharmaceutical products Pharm. Sci. Technol. 3 2000 129 137
    • (2000) Pharm. Sci. Technol. , vol.3 , pp. 129-137
    • Parkins, D.A.1    Lashmar, U.T.2
  • 21
    • 15244343628 scopus 로고    scopus 로고
    • L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
    • R.C. Reddy, H. Lilie, R. Rudolph, and C. Lange l-Arginine increases the solubility of unfolded species of hen egg white lysozyme Prot. Sci. 14 2005 929 935
    • (2005) Prot. Sci. , vol.14 , pp. 929-935
    • Reddy, R.C.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 22
    • 0001664170 scopus 로고
    • The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds
    • D.R. Robinson, and W.P. Jencks The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds J. Am. Chem. Soc. 87 1965 2462 2470
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2462-2470
    • Robinson, D.R.1    Jencks, W.P.2
  • 23
    • 70350755992 scopus 로고    scopus 로고
    • Thermodynamic study of the influence of polyols and glucose on the thermal stability of holo-bovine α-lactalbumin
    • C.M. Romero, A. Albis, J.M. Lozano, and J. Sancho Thermodynamic study of the influence of polyols and glucose on the thermal stability of holo-bovine α-lactalbumin J. Therm. Anal. Calorim. 98 2009 165 171
    • (2009) J. Therm. Anal. Calorim. , vol.98 , pp. 165-171
    • Romero, C.M.1    Albis, A.2    Lozano, J.M.3    Sancho, J.4
  • 24
    • 0026631716 scopus 로고
    • Increased thermal stability of proteins in the presence of naturally occurring osmolytes
    • M.M. Santoro, Y. Liu, S.M.A. Khan, L.X. Hou, and D.W. Bolen Increased thermal stability of proteins in the presence of naturally occurring osmolytes Biochemistry 31 1992 5278 5283
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1    Liu, Y.2    Khan, S.M.A.3    Hou, L.X.4    Bolen, D.W.5
  • 25
    • 79952753113 scopus 로고    scopus 로고
    • Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins
    • D. Shukla, and B.L. Trout Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins J. Phys. Chem. B 115 2011 1243 1253
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1243-1253
    • Shukla, D.1    Trout, B.L.2
  • 26
    • 79251618192 scopus 로고    scopus 로고
    • Protein and DNA destabilization by osmolytes: The other side of the coin
    • L.R. Singh, N.K. Poddar, T.A. Dar, R. Kumar, and F. Ahmad Protein and DNA destabilization by osmolytes: the other side of the coin Life Sci. 88 2011 117 125
    • (2011) Life Sci. , vol.88 , pp. 117-125
    • Singh, L.R.1    Poddar, N.K.2    Dar, T.A.3    Kumar, R.4    Ahmad, F.5
  • 27
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • T.O. Street, D.W. Bolen, and G.D. Rose A molecular mechanism for osmolyte-induced protein stability Proc. Natl. Acad. Sci. U. S. A. 103 2006 13996 14002
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13996-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 28
    • 84864055322 scopus 로고    scopus 로고
    • Excipients differentially influence the conformational stability and pretransition dynamics of two IgG1 monoclonal antibodies
    • S.V. Thakkar, S.B. Joshi, M.E. Jones, H.A. Sathish, S.M. Bishop, D.B. Volkin, and C.R. Middaugh Excipients differentially influence the conformational stability and pretransition dynamics of two IgG1 monoclonal antibodies J. Pharm. Sci. 101 2012 3062 3077
    • (2012) J. Pharm. Sci. , vol.101 , pp. 3062-3077
    • Thakkar, S.V.1    Joshi, S.B.2    Jones, M.E.3    Sathish, H.A.4    Bishop, S.M.5    Volkin, D.B.6    Middaugh, C.R.7
  • 29
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding and preferential hydration
    • S.N. Timasheff Protein hydration, thermodynamic binding and preferential hydration Biochemistry 41 2002 13473 13482
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 31
    • 0344845290 scopus 로고    scopus 로고
    • The guanidine like effects of arginine on aminoacylase and salt-induced molten globule state
    • Q. Xie, T. Guo, J. Lu, and H.M. Zhou The guanidine like effects of arginine on aminoacylase and salt-induced molten globule state Int. J. Biochem. Cell B 36 2004 296 306
    • (2004) Int. J. Biochem. Cell B , vol.36 , pp. 296-306
    • Xie, Q.1    Guo, T.2    Lu, J.3    Zhou, H.M.4
  • 32
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • P.H. Yancey, M.E. Clark, R. Hand, R.D. Bowlus, and G.N. Somero Living with water stress: evolution of osmolyte systems Science 217 1982 1214 1222
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, R.3    Bowlus, R.D.4    Somero, G.N.5


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