메뉴 건너뛰기




Volumn 102, Issue 4, 2013, Pages 1182-1193

Polar solvents decrease the viscosity of high concentration IgG1 solutions through hydrophobic solvation and interaction: Formulation and biocompatibility considerations

Author keywords

Calorimetry; Formulation; High concentration; Immunoglobulin; Monoclonal antibody; Preferential interaction; Protein; Spectroscopy; Viscosity

Indexed keywords

DIMETHYL SULFOXIDE; IMMUNOGLOBULIN G1; N,N DIMETHYLACETAMIDE; SOLVENT;

EID: 84874719195     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23453     Document Type: Article
Times cited : (20)

References (40)
  • 1
    • 70449704158 scopus 로고    scopus 로고
    • Formulation and manufacturability of biologics
    • Shire SJ. 2009. Formulation and manufacturability of biologics. Curr Opin Biotechnol 20:708-714.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 708-714
    • Shire, S.J.1
  • 2
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93:1390-1402.
    • (2004) J Pharm Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 3
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • Yadav S, Liu J, Shire SJ, Kalonia DS. 2010. Specific interactions in high concentration antibody solutions resulting in high viscosity. J Pharm Sci 99:1152-1168.
    • (2010) J Pharm Sci , vol.99 , pp. 1152-1168
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 4
    • 66349132473 scopus 로고    scopus 로고
    • Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties
    • Kamerzell TJ, Kanai S, Liu J, Shire SJ, Wang YJ. 2009. Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties. J Phys Chem B 113:6109-6118.
    • (2009) J Phys Chem B , vol.113 , pp. 6109-6118
    • Kamerzell, T.J.1    Kanai, S.2    Liu, J.3    Shire, S.J.4    Wang, Y.J.5
  • 5
    • 55749113694 scopus 로고    scopus 로고
    • Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity
    • Kanai S, Liu J, Patapoff TW, Shire SJ. 2008. Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity. J Pharm Sci 97:4219-4227.
    • (2008) J Pharm Sci , vol.97 , pp. 4219-4227
    • Kanai, S.1    Liu, J.2    Patapoff, T.W.3    Shire, S.J.4
  • 6
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nguyen MD, Andya JD, Shire SJ. 2005. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J Pharm Sci 94:1928-1940.
    • (2005) J Pharm Sci , vol.94 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.2    Andya, J.D.3    Shire, S.J.4
  • 7
    • 85030486733 scopus 로고    scopus 로고
    • Reduced-viscosity concentrated protein formulations. Patent US6875432B2.
    • Liu J, Shire SJ. 2006. Reduced-viscosity concentrated protein formulations. Patent US6875432B2.
    • (2006)
    • Liu, J.1    Shire, S.J.2
  • 8
    • 78049509357 scopus 로고    scopus 로고
    • Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies
    • Yadav S, Shire SJ, Kalonia DS. 2010. Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies. J Pharm Sci 99:4812-4829.
    • (2010) J Pharm Sci , vol.99 , pp. 4812-4829
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 9
    • 77957843464 scopus 로고    scopus 로고
    • Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering
    • Scherer TM, Liu J, Shire SJ, Minton AP. 2010. Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering. J Phys Chem B 114:12948-12957.
    • (2010) J Phys Chem B , vol.114 , pp. 12948-12957
    • Scherer, T.M.1    Liu, J.2    Shire, S.J.3    Minton, A.P.4
  • 10
    • 62349120772 scopus 로고    scopus 로고
    • Preferential solvation of lysozyme by dimethyl sulfoxide in binary solutions of water and dimethyl sulfoxide
    • Kamiyama T, Liu HL, Kimura T. 2009. Preferential solvation of lysozyme by dimethyl sulfoxide in binary solutions of water and dimethyl sulfoxide. J Therm Anal Calorim 95:353-359.
    • (2009) J Therm Anal Calorim , vol.95 , pp. 353-359
    • Kamiyama, T.1    Liu, H.L.2    Kimura, T.3
  • 11
    • 49149094036 scopus 로고    scopus 로고
    • Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO
    • Duarte AM, van Mierlo CP, Hemminga MA. 2008. Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO. J Phys Chem B 112:8664-8671.
    • (2008) J Phys Chem B , vol.112 , pp. 8664-8671
    • Duarte, A.M.1    van Mierlo, C.P.2    Hemminga, M.A.3
  • 12
    • 0030835825 scopus 로고    scopus 로고
    • Preferential solvation changes upon lysozyme heat denaturation in mixed solvents
    • Kovrigin EL, Potekhin SA. 1997. Preferential solvation changes upon lysozyme heat denaturation in mixed solvents. Biochemistry 36:9195-9199.
    • (1997) Biochemistry , vol.36 , pp. 9195-9199
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 13
    • 0344720263 scopus 로고    scopus 로고
    • Dimethyl sulfoxide binding to globular proteins: A nuclear magnetic relaxation dispersion study
    • Johannesson H, Denisov VP, Halle B. 1997. Dimethyl sulfoxide binding to globular proteins: A nuclear magnetic relaxation dispersion study. Protein Sci 6:1756-1763.
    • (1997) Protein Sci , vol.6 , pp. 1756-1763
    • Johannesson, H.1    Denisov, V.P.2    Halle, B.3
  • 14
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler D. 2005. Interfaces and the driving force of hydrophobic assembly. Nature 437:640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 16
    • 0018414953 scopus 로고
    • Physico-chemical properties and local toxic effects of injectables
    • Oshida S, Degawa K, Takahashi Y, Akaishi S. 1979. Physico-chemical properties and local toxic effects of injectables. Tohoku J Exp Med 127:301-316.
    • (1979) Tohoku J Exp Med , vol.127 , pp. 301-316
    • Oshida, S.1    Degawa, K.2    Takahashi, Y.3    Akaishi, S.4
  • 18
    • 1242337285 scopus 로고    scopus 로고
    • Solubilizing excipients in oral and injectable formulations
    • Strickley RG. 2004. Solubilizing excipients in oral and injectable formulations. Pharm Res 21:201-230.
    • (2004) Pharm Res , vol.21 , pp. 201-230
    • Strickley, R.G.1
  • 19
    • 0016699207 scopus 로고
    • Macromolecular binding
    • Schellman JA. 1975. Macromolecular binding. Biopolymers 14:999-1018.
    • (1975) Biopolymers , vol.14 , pp. 999-1018
    • Schellman, J.A.1
  • 20
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman JA. 1990. A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. Biophys Chem 37:121-140.
    • (1990) Biophys Chem , vol.37 , pp. 121-140
    • Schellman, J.A.1
  • 21
    • 0029034433 scopus 로고
    • An osmolyte effect on the heat capacity change for protein folding
    • Plaza del Pino IM, Sanchez-Ruiz JM. 1995. An osmolyte effect on the heat capacity change for protein folding. Biochemistry 34:8621-8630.
    • (1995) Biochemistry , vol.34 , pp. 8621-8630
    • Plaza del Pino, I.M.1    Sanchez-Ruiz, J.M.2
  • 22
    • 0033992112 scopus 로고    scopus 로고
    • On the stabilizing action of protein denaturants: Acetonitrile effect on stability of lysozyme in aqueous solutions
    • Kovrigin EL, Potekhin SA. 2000. On the stabilizing action of protein denaturants: Acetonitrile effect on stability of lysozyme in aqueous solutions. Biophys Chem 83:45-59.
    • (2000) Biophys Chem , vol.83 , pp. 45-59
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 23
    • 0041336626 scopus 로고    scopus 로고
    • Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study
    • Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR. 2003. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. J Pharm Sci 92:1805-1820.
    • (2003) J Pharm Sci , vol.92 , pp. 1805-1820
    • Kueltzo, L.A.1    Ersoy, B.2    Ralston, J.P.3    Middaugh, C.R.4
  • 24
    • 1542502033 scopus 로고    scopus 로고
    • Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme
    • Kovrigin EL, Potekhin SA. 1996. Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme. Biofizika 41:1201-1206.
    • (1996) Biofizika , vol.41 , pp. 1201-1206
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 25
    • 0030175847 scopus 로고    scopus 로고
    • Molecular dynamics of subtilisin Carlsberg in aqueous and nonaqueous solutions
    • Zheng YJ, Ornstein RL. 1996. Molecular dynamics of subtilisin Carlsberg in aqueous and nonaqueous solutions. Biopolymers 38:791-799.
    • (1996) Biopolymers , vol.38 , pp. 791-799
    • Zheng, Y.J.1    Ornstein, R.L.2
  • 26
    • 36849073223 scopus 로고    scopus 로고
    • Raman spectroscopy of protein pharmaceuticals
    • Wen ZQ. 2007. Raman spectroscopy of protein pharmaceuticals. J Pharm Sci 96:2861-2878.
    • (2007) J Pharm Sci , vol.96 , pp. 2861-2878
    • Wen, Z.Q.1
  • 28
    • 0031555514 scopus 로고    scopus 로고
    • Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents
    • Xu K, Griebenow K, Klibanov AM. 1997. Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents. Biotechnol Bioeng 56:485-491.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 485-491
    • Xu, K.1    Griebenow, K.2    Klibanov, A.M.3
  • 29
    • 0028946517 scopus 로고
    • Effects of dimethyl sulfoxide, glycerol, and ethylene glycol on secondary structures of cytochrome c and lysozyme as observed by infrared spectroscopy
    • Huang P, Dong A, Caughey WS. 1995. Effects of dimethyl sulfoxide, glycerol, and ethylene glycol on secondary structures of cytochrome c and lysozyme as observed by infrared spectroscopy. J Pharm Sci 84:387-392.
    • (1995) J Pharm Sci , vol.84 , pp. 387-392
    • Huang, P.1    Dong, A.2    Caughey, W.S.3
  • 30
    • 0033586348 scopus 로고    scopus 로고
    • Protein refolding in predominantly organic media markedly enhanced by common salts
    • Rariy RV, Klibanov AM. 1999. Protein refolding in predominantly organic media markedly enhanced by common salts. Biotechnol Bioeng 62:704-710.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 704-710
    • Rariy, R.V.1    Klibanov, A.M.2
  • 31
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A, Zscherp C. 2002. What vibrations tell us about proteins. Q Rev Biophys 35:369-430.
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 32
    • 0014590038 scopus 로고
    • Behavior of erythrocytes in various solvent systems. V. Water-liquid amides
    • Cadwallader DE, Phillips JR. 1969. Behavior of erythrocytes in various solvent systems. V. Water-liquid amides. J Pharm Sci 58:1220-1224.
    • (1969) J Pharm Sci , vol.58 , pp. 1220-1224
    • Cadwallader, D.E.1    Phillips, J.R.2
  • 33
    • 15644383223 scopus 로고    scopus 로고
    • Lysis of human red blood cells. 4. Comparison of in vitro and in vivo hemolysis data
    • Krzyzaniak JF, Alvarez Nunez FA, Raymond DM, Yalkowsky SH. 1997. Lysis of human red blood cells. 4. Comparison of in vitro and in vivo hemolysis data. J Pharm Sci 86:1215-1217.
    • (1997) J Pharm Sci , vol.86 , pp. 1215-1217
    • Krzyzaniak, J.F.1    Alvarez, N.F.2    Raymond, D.M.3    Yalkowsky, S.H.4
  • 34
    • 33745044984 scopus 로고    scopus 로고
    • In vitro hemolysis: Guidance for the pharmaceutical scientist
    • Amin K, Dannenfelser RM. 2006. In vitro hemolysis: Guidance for the pharmaceutical scientist. J Pharm Sci 95:1173-1176.
    • (2006) J Pharm Sci , vol.95 , pp. 1173-1176
    • Amin, K.1    Dannenfelser, R.M.2
  • 35
    • 0022203690 scopus 로고
    • Medical use of dimethyl sulfoxide (DMSO)
    • Swanson BN. 1985. Medical use of dimethyl sulfoxide (DMSO). Rev Clin Basic Pharm 5:1-33.
    • (1985) Rev Clin Basic Pharm , vol.5 , pp. 1-33
    • Swanson, B.N.1
  • 36
    • 0028673929 scopus 로고
    • Dimethyl sulphoxide: A review of its applications in cell biology
    • Yu ZW, Quinn PJ. 1994. Dimethyl sulphoxide: A review of its applications in cell biology. Biosci Rep 14:259-281.
    • (1994) Biosci Rep , vol.14 , pp. 259-281
    • Yu, Z.W.1    Quinn, P.J.2
  • 37
    • 0013799389 scopus 로고
    • Observations on the pharmacology and hemolytic activity of dimethyl sulfoxide
    • DiStefano V, Klahn JJ. 1965. Observations on the pharmacology and hemolytic activity of dimethyl sulfoxide. Toxicol Appl Pharmacol 7:660-666.
    • (1965) Toxicol Appl Pharmacol , vol.7 , pp. 660-666
    • DiStefano, V.1    Klahn, J.J.2
  • 38
    • 0014203880 scopus 로고
    • The metabolism of dimethyl sulfoxide and its metabolic effects in man and animals
    • Gerhards E, Gibian H. 1967. The metabolism of dimethyl sulfoxide and its metabolic effects in man and animals. Ann N Y Acad Sci 141:65-76.
    • (1967) Ann N Y Acad Sci , vol.141 , pp. 65-76
    • Gerhards, E.1    Gibian, H.2
  • 39
    • 0033067940 scopus 로고    scopus 로고
    • Characterization and comparison of leuprolide degradation profiles in water and dimethyl sulfoxide
    • Hall SC, Tan MM, Leonard JJ, Stevenson CL. 1999. Characterization and comparison of leuprolide degradation profiles in water and dimethyl sulfoxide. J Pept Res 53:432-441.
    • (1999) J Pept Res , vol.53 , pp. 432-441
    • Hall, S.C.1    Tan, M.M.2    Leonard, J.J.3    Stevenson, C.L.4
  • 40
    • 0032723035 scopus 로고    scopus 로고
    • Effect of peptide concentration and temperature on leuprolide stability in dimethyl sulfoxide
    • Stevenson CL, Leonard JJ, Hall SC. 1999. Effect of peptide concentration and temperature on leuprolide stability in dimethyl sulfoxide. Int J Pharm 191:115-129.
    • (1999) Int J Pharm , vol.191 , pp. 115-129
    • Stevenson, C.L.1    Leonard, J.J.2    Hall, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.