메뉴 건너뛰기




Volumn 7, Issue 9, 2009, Pages 32-44

Large-scale freezing of biologics

Author keywords

Aggregation; Bulk intermediates; Denaturation; Eutectic, storage; Stability; TG; Transport

Indexed keywords

EXCIPIENT; GLYCINE; LACTATE DEHYDROGENASE; MACROGOL; MANNITOL; MYOGLOBIN; OVALBUMIN; STABILIZING AGENT; SURFACTANT; WATER;

EID: 77951977681     PISSN: 15426319     EISSN: None     Source Type: Trade Journal    
DOI: None     Document Type: Review
Times cited : (64)

References (50)
  • 1
    • 45149102199 scopus 로고    scopus 로고
    • Storage Consideration As Part of the Formulation Development Program for Biologics
    • Singh SK. Storage Consideration As Part of the Formulation Development Program for Biologics. Amer. Pharmaceut. Rev. 10(3) 2007: 26-33.
    • (2007) Amer. Pharmaceut. Rev , vol.10 , Issue.3 , pp. 26-33
    • Singh, S.K.1
  • 2
    • 70449712980 scopus 로고    scopus 로고
    • Best Practices for Formulation and Manufacturing of Biotech Drug Products
    • Singh SK, et al. Best Practices for Formulation and Manufacturing of Biotech Drug Products. BioPharm Int. 22(6) 2009: 32-48.
    • (2009) BioPharm Int , vol.22 , Issue.6 , pp. 32-48
    • Singh, S.K.1
  • 3
    • 0028925570 scopus 로고
    • Protein Destabilization at Low Temperatures
    • Franks F. Protein Destabilization at Low Temperatures. Adv. Protein Chem. 46, 1995: 105-139.
    • (1995) Adv. Protein Chem , vol.46 , pp. 105-139
    • Franks, F.1
  • 4
    • 0038700496 scopus 로고    scopus 로고
    • Nucleation of Ice and Its Management in Ecosystems
    • Franks F. Nucleation of Ice and Its Management in Ecosystems. Phil. Trans. Royal Soc. London, A. 361, 2003: 557-574.
    • (2003) Phil. Trans. Royal Soc. London, A , vol.361 , pp. 557-574
    • Franks, F.1
  • 5
    • 35748979712 scopus 로고    scopus 로고
    • Protein Stability During Freezing: Separation of Stresses and Mechanisms of Protein Stabilization
    • Bhatnagar B, Bogner RH, Pikal MJ. Protein Stability During Freezing: Separation of Stresses and Mechanisms of Protein Stabilization. Pharm. Dev. Technol. 12, 2007: 505-523.
    • (2007) Pharm. Dev. Technol , vol.12 , pp. 505-523
    • Bhatnagar, B.1    Bogner, R.H.2    Pikal, M.J.3
  • 6
    • 0016204251 scopus 로고
    • Phase Diagram Relationships in Cryobiology
    • Cocks FH, Brower WE. Phase Diagram Relationships in Cryobiology. Cryobiol. 11, 1974: 340-358.
    • (1974) Cryobiol , vol.11 , pp. 340-358
    • Cocks, F.H.1    Brower, W.E.2
  • 7
    • 0026411964 scopus 로고    scopus 로고
    • Roos Y, Karel M. Applying State Diagrams to Food Processing and Development. Food Technol. 45, 1991: 66-71, 107.
    • Roos Y, Karel M. Applying State Diagrams to Food Processing and Development. Food Technol. 45, 1991: 66-71, 107.
  • 8
    • 0036319970 scopus 로고    scopus 로고
    • Calculation of the Cg? and Tg? Interaction Point in the State Diagram of Frozen Solutions
    • Matveev YI, Ablett S. Calculation of the Cg? and Tg? Interaction Point in the State Diagram of Frozen Solutions. Food Hydrocoll. 16, 2002: 419-422.
    • (2002) Food Hydrocoll , vol.16 , pp. 419-422
    • Matveev, Y.I.1    Ablett, S.2
  • 9
    • 0345732482 scopus 로고
    • The H2O-NaCl-Sucrose Phase Diagram and Applications in Cryobiology
    • Gayle FW, Cocks FH, Shepard ML. The H2O-NaCl-Sucrose Phase Diagram and Applications in Cryobiology. J. Appl. Chem. Biotechnol. 27, 1977: 599-607.
    • (1977) J. Appl. Chem. Biotechnol , vol.27 , pp. 599-607
    • Gayle, F.W.1    Cocks, F.H.2    Shepard, M.L.3
  • 10
    • 17444419893 scopus 로고    scopus 로고
    • The Water to Ice Transition: Implications for Living Cells
    • Fuller BJ, Benson EF, Lane N, Eds. CRC Press: Boca Raton, FL
    • Muldrew K, et al. The Water to Ice Transition: Implications for Living Cells. Life in the Frozen State. Fuller BJ, Benson EF, Lane N, Eds. CRC Press: Boca Raton, FL, 2004: 67-108.
    • (2004) Life in the Frozen State , pp. 67-108
    • Muldrew, K.1
  • 11
    • 36048943434 scopus 로고    scopus 로고
    • accessed August 2009
    • Chaplin M. Protein Hydration, 2008; www.lsbu.ac.uk/water/protein. html#r1197; accessed August 2009.
    • (2008) Protein Hydration
    • Chaplin, M.1
  • 12
    • 6844241962 scopus 로고    scopus 로고
    • Real Time In Situ Monitoring of Lysozyme During Lyophilization Using Infrared Spectroscopy: Dehydration Stress in the Presence of Sucrose
    • Remmele RL, Stushnoff C, Carpenter JF. Real Time In Situ Monitoring of Lysozyme During Lyophilization Using Infrared Spectroscopy: Dehydration Stress in the Presence of Sucrose. Pharm. Res. 14, 1997: 1548-1555.
    • (1997) Pharm. Res , vol.14 , pp. 1548-1555
    • Remmele, R.L.1    Stushnoff, C.2    Carpenter, J.F.3
  • 13
    • 0035981605 scopus 로고    scopus 로고
    • Thermodynamic Quantities for the Ionization Reaction of Buffers
    • Goldberg RN, Kishore N, Lennen RM. Thermodynamic Quantities for the Ionization Reaction of Buffers. J. Phys. Chem. Ref. Data 31(2) 2002: 231-370.
    • (2002) J. Phys. Chem. Ref. Data , vol.31 , Issue.2 , pp. 231-370
    • Goldberg, R.N.1    Kishore, N.2    Lennen, R.M.3
  • 14
    • 77953416654 scopus 로고    scopus 로고
    • Larsen SS. Studies on Stability of Drugs in Frozen Systems, VI: The Effect of Freezing upon pH for Buffered Aqueous Solutions. Arch. Pharm. Chemi. Sci. Ed. 1, 1973: 41-53.
    • Larsen SS. Studies on Stability of Drugs in Frozen Systems, VI: The Effect of Freezing upon pH for Buffered Aqueous Solutions. Arch. Pharm. Chemi. Sci. Ed. 1, 1973: 41-53.
  • 15
    • 77953430310 scopus 로고    scopus 로고
    • Impact of Freezing upon pH of Buffered Solutions and Consequences for Monoclonal Antibody Aggregation
    • submitted
    • Kolhe P, Amend E, Singh SK. Impact of Freezing upon pH of Buffered Solutions and Consequences for Monoclonal Antibody Aggregation. Biotechnol. Prog. 2009: submitted.
    • (2009) Biotechnol. Prog
    • Kolhe, P.1    Amend, E.2    Singh, S.K.3
  • 16
    • 77953438131 scopus 로고    scopus 로고
    • Cromwell M. Opalescence: A Clarifying Case Study. IBC's Fourth Annual BioProcess International European Conference and Exhibition: Vienna, Austria, 21-24 April 2008.
    • Cromwell M. Opalescence: A Clarifying Case Study. IBC's Fourth Annual BioProcess International European Conference and Exhibition: Vienna, Austria, 21-24 April 2008.
  • 17
    • 77953439418 scopus 로고    scopus 로고
    • Methods for Reducing or Preventing Liquid-Liquid Phase Separation in High Concentration Protein Solutions
    • US patent application /0070230 A1: 2008; www.wipo.int/pctdb/en/wo.jsp?WO= 2007146268
    • Li L, Kantor A, Warne NW. Methods for Reducing or Preventing Liquid-Liquid Phase Separation in High Concentration Protein Solutions. US patent application 2008/0070230 A1: 2008; www.wipo.int/pctdb/en/wo.jsp?WO= 2007146268.
    • (2008)
    • Li, L.1    Kantor, A.2    Warne, N.W.3
  • 18
    • 33751552849 scopus 로고
    • Liquid-Liquid Phase Separation of Aqueous Lysozyme Solutions: Effects of pH and Salt Identity
    • Taratuta VG, et al. Liquid-Liquid Phase Separation of Aqueous Lysozyme Solutions: Effects of pH and Salt Identity. J. Phys. Chem. 94, 1990: 2140-2144.
    • (1990) J. Phys. Chem , vol.94 , pp. 2140-2144
    • Taratuta, V.G.1
  • 19
    • 0037172992 scopus 로고    scopus 로고
    • Liquid-Liquid Separation in Solutions of Normal and Sickle Cell Hemoglobin
    • Galkin O, et al. Liquid-Liquid Separation in Solutions of Normal and Sickle Cell Hemoglobin. Proc. Natl. Acad. Sci. 99, 2002: 8479-8483.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 8479-8483
    • Galkin, O.1
  • 20
    • 0023430928 scopus 로고
    • Binary Liquid Phase Separation and Critical Phenomena in a Protein/Water Solution
    • Thomson JA, et al. Binary Liquid Phase Separation and Critical Phenomena in a Protein/Water Solution. Proc. Natl. Acad. Sci. 84, 1987: 7079-7083.
    • (1987) Proc. Natl. Acad. Sci , vol.84 , pp. 7079-7083
    • Thomson, J.A.1
  • 21
    • 33646007703 scopus 로고    scopus 로고
    • Shen VK, et al. Coarse-Grained Strategy for Modeling Protein Stability in Concentrated Solutions, II: Phase Behavior. Biophys. J. 90, 2006: 1949-1960.
    • Shen VK, et al. Coarse-Grained Strategy for Modeling Protein Stability in Concentrated Solutions, II: Phase Behavior. Biophys. J. 90, 2006: 1949-1960.
  • 22
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in Frozen Solutions: Evidence of Ice-Induced Partial Unfolding
    • Strambini GB, Gabellieri E. Proteins in Frozen Solutions: Evidence of Ice-Induced Partial Unfolding. Biophys. J. 70, 1996: 971-976.
    • (1996) Biophys. J , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 23
    • 0030443567 scopus 로고    scopus 로고
    • Surface-Induced Denaturation of Proteins During Freezing and Its Inhibition By Surfactants
    • Chang BS, Kendrick BS, Carpenter JF. Surface-Induced Denaturation of Proteins During Freezing and Its Inhibition By Surfactants. J. Pharm. Sci. 85, 1996: 1325-1330.
    • (1996) J. Pharm. Sci , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 24
    • 33947627702 scopus 로고    scopus 로고
    • Protein Stability in Ice
    • Strambini GB, Gonnelli M. Protein Stability in Ice. Biophys. J. 92, 2007: 2131-2138.
    • (2007) Biophys. J , vol.92 , pp. 2131-2138
    • Strambini, G.B.1    Gonnelli, M.2
  • 26
    • 0001571730 scopus 로고
    • Stability of Proteins at Subzero Temperatures: Thermodynamics and Some Ecological Consequences
    • Franks F, Hatley RHM. Stability of Proteins at Subzero Temperatures: Thermodynamics and Some Ecological Consequences. Pure Appl. Chem. 63, 1991: 1367-1380.
    • (1991) Pure Appl. Chem , vol.63 , pp. 1367-1380
    • Franks, F.1    Hatley, R.H.M.2
  • 30
    • 0024456040 scopus 로고
    • The Cold-Induced Denaturation of Lactate Dehydrogenase at Sub-Zero Temperatures in the Absence of Perturbants
    • Hatley RHM, Franks F. The Cold-Induced Denaturation of Lactate Dehydrogenase at Sub-Zero Temperatures in the Absence of Perturbants. FEBS Lett. 257, 1989: 171-173.
    • (1989) FEBS Lett , vol.257 , pp. 171-173
    • Hatley, R.H.M.1    Franks, F.2
  • 31
    • 0008530768 scopus 로고
    • Cold Denaturation of Staphylococcal Nuclease
    • Griko YV, et al. Cold Denaturation of Staphylococcal Nuclease. Proc. Natl. Acad. Sci. USA. 85, 1988: 3343-3347.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3343-3347
    • Griko, Y.V.1
  • 33
    • 0035854688 scopus 로고    scopus 로고
    • Structural Determinants of Cold Adaptation and Stability in a Large Protein
    • D'Amico S, Gerday C, Fellert G. Structural Determinants of Cold Adaptation and Stability in a Large Protein. J. Biol. Chem. 276, 2001: 25791-25796.
    • (2001) J. Biol. Chem , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Fellert, G.3
  • 34
    • 4344622456 scopus 로고    scopus 로고
    • Conformational Stability and Thermodynamic Characterization of the Lipoic Acid Bearing Domain of the Human Mitochondrial Branched Chain ?-Ketoacid Dehydrogenase
    • Naik MT, Huang T-H. Conformational Stability and Thermodynamic Characterization of the Lipoic Acid Bearing Domain of the Human Mitochondrial Branched Chain ?-Ketoacid Dehydrogenase. Protein Sci. 13, 2004: 2483-2492.
    • (2004) Protein Sci , vol.13 , pp. 2483-2492
    • Naik, M.T.1    Huang, T.-H.2
  • 35
    • 23744490027 scopus 로고    scopus 로고
    • The Effect of Stabilizers and Denaturants on the Cold Denaturation Temperatures of Proteins and Implications for Freeze Drying
    • Tang X, Pikal MJ. The Effect of Stabilizers and Denaturants on the Cold Denaturation Temperatures of Proteins and Implications for Freeze Drying. Pharm. Res. 22, 2005: 1167-1175.
    • (2005) Pharm. Res , vol.22 , pp. 1167-1175
    • Tang, X.1    Pikal, M.J.2
  • 36
    • 85009900563 scopus 로고
    • Glass Transitions and Product Stability: An Overview
    • Schenz TW. Glass Transitions and Product Stability: An Overview. Food Hydrocoll. 9, 1995: 307-315.
    • (1995) Food Hydrocoll , vol.9 , pp. 307-315
    • Schenz, T.W.1
  • 37
    • 33845410077 scopus 로고    scopus 로고
    • Sorbitol Crystallization Can Lead to Protein Aggregation in the Frozen State
    • Piedmonte DM, et al. Sorbitol Crystallization Can Lead to Protein Aggregation in the Frozen State. Pharm. Res. 24, 2006: 136-146.
    • (2006) Pharm. Res , vol.24 , pp. 136-146
    • Piedmonte, D.M.1
  • 38
    • 48549086114 scopus 로고    scopus 로고
    • Effect of Solution Conditions, Processing Parameters and Container Materials on Aggregation of a Monoclonal Antibody During Freeze Thawing
    • Kueltzo LA, et al. Effect of Solution Conditions, Processing Parameters and Container Materials on Aggregation of a Monoclonal Antibody During Freeze Thawing. J. Pharm. Sci. 97(5) 2008: 1801-1812.
    • (2008) J. Pharm. Sci , vol.97 , Issue.5 , pp. 1801-1812
    • Kueltzo, L.A.1
  • 39
    • 37049068040 scopus 로고
    • Thermomechanical Properties of Small Carbohydrate-Water Glasses and Rubbers: Kinetically Metastable Systems at Sub-Zero Temperatures
    • Levine H, Slade L. Thermomechanical Properties of Small Carbohydrate-Water Glasses and Rubbers: Kinetically Metastable Systems at Sub-Zero Temperatures. J. Chem. Soc. Faraday Trans. I. 84, 1988a: 2619-2633.
    • (1988) J. Chem. Soc. Faraday Trans. I , vol.84 , pp. 2619-2633
    • Levine, H.1    Slade, L.2
  • 40
    • 0001962269 scopus 로고
    • Principles of "Cryostabilization" Technology from Structure/Property Relationships of Carbohydrate/Water Systems: A Review
    • Levine H, Slade L. Principles of "Cryostabilization" Technology from Structure/Property Relationships of Carbohydrate/Water Systems: A Review. Cryolett. 9, 1988b: 21-63.
    • (1988) Cryolett , vol.9 , pp. 21-63
    • Levine, H.1    Slade, L.2
  • 41
    • 37049085493 scopus 로고
    • Differential Scanning Calorimetric Study of Frozen Sucrose and Glycerol Solutions
    • Ablett S, Izzard MJ, Lillford PJ. Differential Scanning Calorimetric Study of Frozen Sucrose and Glycerol Solutions. J. Chem. Soc. Faraday Trans. I. 1992, 789-794.
    • (1992) J. Chem. Soc. Faraday Trans. I , pp. 789-794
    • Ablett, S.1    Izzard, M.J.2    Lillford, P.J.3
  • 42
    • 0000818501 scopus 로고
    • Use of Subambient Thermal Analysis to Optimize Protein Lyophilization
    • Chang BS, Randall CS. Use of Subambient Thermal Analysis to Optimize Protein Lyophilization. Cryobiol. 29, 1992: 632-656.
    • (1992) Cryobiol , vol.29 , pp. 632-656
    • Chang, B.S.1    Randall, C.S.2
  • 44
    • 0022743346 scopus 로고
    • The Effects of Cooling Rate on Solid Phase Transitions and Associated Vial Breakage Occurring in Frozen Mannitol Solutions
    • Williams NA, et al. The Effects of Cooling Rate on Solid Phase Transitions and Associated Vial Breakage Occurring in Frozen Mannitol Solutions. PDA J. Parenter. Sci. Technol. 40, 1986: 135-141.
    • (1986) PDA J. Parenter. Sci. Technol , vol.40 , pp. 135-141
    • Williams, N.A.1
  • 45
    • 34547223487 scopus 로고    scopus 로고
    • Vial Breakage During Freeze-Drying: Crystallization of Sodium Chloride in Sodium Chloride-Sucrose Frozen Aqueous Solutions
    • Milton N, et al. Vial Breakage During Freeze-Drying: Crystallization of Sodium Chloride in Sodium Chloride-Sucrose Frozen Aqueous Solutions. J. Pharm. Sci. 96, 2007: 1848-1853.
    • (2007) J. Pharm. Sci , vol.96 , pp. 1848-1853
    • Milton, N.1
  • 46
    • 0023905575 scopus 로고
    • The Mechanism of Cryoprotection of Proteins by Solutes
    • Carpenter JF, Crowe JH. The Mechanism of Cryoprotection of Proteins by Solutes. Cryobiol. 25, 1988: 244-255.
    • (1988) Cryobiol , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 47
    • 0025732448 scopus 로고
    • Protein-Solvent Interactions in Pharmaceutical Formulations
    • Arakawa T, Kita Y, Carpenter JF. Protein-Solvent Interactions in Pharmaceutical Formulations. Pharm. Res. 8, 1991: 285-291.
    • (1991) Pharm. Res , vol.8 , pp. 285-291
    • Arakawa, T.1    Kita, Y.2    Carpenter, J.F.3
  • 48
    • 0027272126 scopus 로고
    • Freeze-Thaw Studies of a Model Protein, Lactate Dehydrogenase, in the Presence of Cryoprotectants
    • Nema S, Avis KE. Freeze-Thaw Studies of a Model Protein, Lactate Dehydrogenase, in the Presence of Cryoprotectants. J. Parenteral Sci. Technol. 47, 1993: 76-83.
    • (1993) J. Parenteral Sci. Technol , vol.47 , pp. 76-83
    • Nema, S.1    Avis, K.E.2
  • 49
    • 0030770631 scopus 로고    scopus 로고
    • Rational Design of Stable Lyophilized Protein Formulations: Some Practical Advice
    • Carpenter JF, et al. Rational Design of Stable Lyophilized Protein Formulations: Some Practical Advice. Pharm. Res. 14, 1997: 969-975.
    • (1997) Pharm. Res , vol.14 , pp. 969-975
    • Carpenter, J.F.1
  • 50
    • 66349137053 scopus 로고    scopus 로고
    • Synchrotron X-Ray Diffraction Investigation of the Anomalous Behavior of Ice During Freezing of Aqueous Systems
    • Varshney DB, et al. Synchrotron X-Ray Diffraction Investigation of the Anomalous Behavior of Ice During Freezing of Aqueous Systems. J. Phys. Chem. B. Lett. 113, 2009: 6177-6182.
    • (2009) J. Phys. Chem. B. Lett , vol.113 , pp. 6177-6182
    • Varshney, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.