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Volumn 119, Issue 49, 2015, Pages 15150-15163

Structural Changes and Aggregation Mechanisms for Anti-Streptavidin IgG1 at Elevated Concentration

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; LIGHT SCATTERING; NEUTRON SCATTERING; PROTEINS; SUGAR (SUCROSE); ULTRAVIOLET SPECTROSCOPY;

EID: 84949568378     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b08748     Document Type: Article
Times cited : (24)

References (74)
  • 1
    • 84921352030 scopus 로고    scopus 로고
    • The Therapeutic Monoclonal Antibody Market
    • Ecker, D. M.; Jones, S. D.; Levine, H. L. The Therapeutic Monoclonal Antibody Market mAbs 2015, 7, 9-14 10.4161/19420862.2015.989042
    • (2015) MAbs , vol.7 , pp. 9-14
    • Ecker, D.M.1    Jones, S.D.2    Levine, H.L.3
  • 3
    • 84897869100 scopus 로고    scopus 로고
    • Immunogenicity of Therapeutic Proteins: Influence of Aggregation
    • Ratanji, K. D.; Derrick, J. P.; Dearman, R. J.; Kimber, I. Immunogenicity of Therapeutic Proteins: Influence of Aggregation J. Immunotoxicol. 2014, 11, 99-109 10.3109/1547691X.2013.821564
    • (2014) J. Immunotoxicol. , vol.11 , pp. 99-109
    • Ratanji, K.D.1    Derrick, J.P.2    Dearman, R.J.3    Kimber, I.4
  • 4
    • 84861337214 scopus 로고    scopus 로고
    • Immunogenicity of Protein aggregates - Concerns and Realities
    • Wang, W.; Singh, S. K.; Li, N.; Toler, M. R.; King, K. R.; Nema, S. Immunogenicity of Protein aggregates - Concerns and Realities Int. J. Pharm. 2012, 431, 1-11 10.1016/j.ijpharm.2012.04.040
    • (2012) Int. J. Pharm. , vol.431 , pp. 1-11
    • Wang, W.1    Singh, S.K.2    Li, N.3    Toler, M.R.4    King, K.R.5    Nema, S.6
  • 6
    • 84929154056 scopus 로고    scopus 로고
    • Antibody Glycosylation and Its Impact on the Pharmacokinetics and Pharmacodynamics of Monoclonal Antibodies and Fc-Fusion Proteins
    • Liu, L. Antibody Glycosylation and Its Impact on the Pharmacokinetics and Pharmacodynamics of Monoclonal Antibodies and Fc-Fusion Proteins J. Pharm. Sci. 2015, 104, 1866-1884 10.1002/jps.24444
    • (2015) J. Pharm. Sci. , vol.104 , pp. 1866-1884
    • Liu, L.1
  • 7
    • 84872490861 scopus 로고    scopus 로고
    • Ionic Strength Affects Tertiary Structure and Aggregation Propensity of a Monoclonal Antibody Adsorbed to Silicone Oil-Water Interfaces
    • Gerhardt, A.; Bonam, K.; Bee, J. S.; Carpenter, J. F.; Randolph, T. W. Ionic Strength Affects Tertiary Structure and Aggregation Propensity of a Monoclonal Antibody Adsorbed to Silicone Oil-Water Interfaces J. Pharm. Sci. 2013, 102, 429-440 10.1002/jps.23408
    • (2013) J. Pharm. Sci. , vol.102 , pp. 429-440
    • Gerhardt, A.1    Bonam, K.2    Bee, J.S.3    Carpenter, J.F.4    Randolph, T.W.5
  • 8
    • 80053289158 scopus 로고    scopus 로고
    • Glass Particles as an Adjuvant: A Model for Adverse Immunogenicity of Therapeutic Proteins
    • Fradkin, A. H.; Carpenter, J. F.; Randolph, T. W. Glass Particles as an Adjuvant: A Model for Adverse Immunogenicity of Therapeutic Proteins J. Pharm. Sci. 2011, 100, 4953-4964 10.1002/jps.22683
    • (2011) J. Pharm. Sci. , vol.100 , pp. 4953-4964
    • Fradkin, A.H.1    Carpenter, J.F.2    Randolph, T.W.3
  • 9
    • 84862893136 scopus 로고    scopus 로고
    • Relationship between Potential Aggregation-Prone Regions and HLA-DR-Binding T-Cell Immune Epitopes: Implications for Rational Design of Novel and Follow-on Therapeutic Antibodies
    • Kumar, S.; Mitchell, M. A.; Rup, B.; Singh, S. K. Relationship between Potential Aggregation-Prone Regions and HLA-DR-Binding T-Cell Immune Epitopes: Implications for Rational Design of Novel and Follow-on Therapeutic Antibodies J. Pharm. Sci. 2012, 101, 2686-2701 10.1002/jps.23169
    • (2012) J. Pharm. Sci. , vol.101 , pp. 2686-2701
    • Kumar, S.1    Mitchell, M.A.2    Rup, B.3    Singh, S.K.4
  • 10
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the Development of High Protein Concentration Formulations
    • Shire, S. J.; Shahrokh, Z.; Liu, J. Challenges in the Development of High Protein Concentration Formulations J. Pharm. Sci. 2004, 93, 1390-1402 10.1002/jps.20079
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 11
    • 84878370686 scopus 로고    scopus 로고
    • Monoclonal Antibody Self-Association, Cluster Formation, and Rheology at High Concentrations
    • Lilyestrom, W. G.; Yadav, S.; Shire, S. J.; Scherer, T. M. Monoclonal Antibody Self-Association, Cluster Formation, and Rheology at High Concentrations J. Phys. Chem. B 2013, 117, 6373-6384 10.1021/jp4008152
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6373-6384
    • Lilyestrom, W.G.1    Yadav, S.2    Shire, S.J.3    Scherer, T.M.4
  • 12
    • 84881463459 scopus 로고    scopus 로고
    • Small-Angle Neutron Scattering Characterization of Monoclonal Antibody Conformations and Interactions at High Concentrations
    • Yearley, E. J.; Zarraga, I. E.; Shire, S. J.; Scherer, T. M.; Gokarn, Y.; Wagner, N. J.; Liu, Y. Small-Angle Neutron Scattering Characterization of Monoclonal Antibody Conformations and Interactions at High Concentrations Biophys. J. 2013, 105, 720-731 10.1016/j.bpj.2013.06.043
    • (2013) Biophys. J. , vol.105 , pp. 720-731
    • Yearley, E.J.1    Zarraga, I.E.2    Shire, S.J.3    Scherer, T.M.4    Gokarn, Y.5    Wagner, N.J.6    Liu, Y.7
  • 13
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the Development of High Protein Concentration Formulations
    • Shire, S. J.; Shahrokh, Z.; Liu, J. Challenges in the Development of High Protein Concentration Formulations J. Pharm. Sci. 2004, 93, 1390-1402 10.1002/jps.20079
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 14
    • 84864131010 scopus 로고    scopus 로고
    • Size-Exclusion Chromatography with Multi-Angle Light Scattering for Elucidating Protein Aggregation Mechanisms
    • Sahin, E.; Roberts, C. J. Size-Exclusion Chromatography with Multi-Angle Light Scattering for Elucidating Protein Aggregation Mechanisms Methods Mol. Biol. 2012, 899, 403-423 10.1007/978-1-61779-921-1-25
    • (2012) Methods Mol. Biol. , vol.899 , pp. 403-423
    • Sahin, E.1    Roberts, C.J.2
  • 15
    • 77951267552 scopus 로고    scopus 로고
    • Potential Inaccurate Quantitation and Sizing of Protein Aggregates by Size Exclusion Chromatography: Essential Need to Use Orthogonal Methods to Assure the Quality of Therapeutic Protein Products
    • Carpenter, J. F.; Randolph, T. W.; Jiskoot, W.; Crommelin, D. J. A.; Middaugh, C. R.; Winter, G. Potential Inaccurate Quantitation and Sizing of Protein Aggregates by Size Exclusion Chromatography: Essential Need to Use Orthogonal Methods to Assure the Quality of Therapeutic Protein Products J. Pharm. Sci. 2010, 99, 2200-2208 10.1002/jps.21989
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2200-2208
    • Carpenter, J.F.1    Randolph, T.W.2    Jiskoot, W.3    Crommelin, D.J.A.4    Middaugh, C.R.5    Winter, G.6
  • 16
    • 84922952911 scopus 로고    scopus 로고
    • Calculating the Mass of Subvisible Protein Particles with Improved Accuracy Using Microflow Imaging Data
    • Kalonia, C.; Kumru, O. S.; Prajapati, I.; Mathaes, R.; Engert, J.; Zhou, S.; Middaugh, C. R.; Volkin, D. B. Calculating the Mass of Subvisible Protein Particles with Improved Accuracy Using Microflow Imaging Data J. Pharm. Sci. 2015, 104, 536-547 10.1002/jps.24156
    • (2015) J. Pharm. Sci. , vol.104 , pp. 536-547
    • Kalonia, C.1    Kumru, O.S.2    Prajapati, I.3    Mathaes, R.4    Engert, J.5    Zhou, S.6    Middaugh, C.R.7    Volkin, D.B.8
  • 17
    • 77955101936 scopus 로고    scopus 로고
    • Development of a Microflow Digital Imaging Assay to Characterize Protein Particulates during Storage of a High Concentration IgG1 Monoclonal Antibody Formulation
    • Wuchner, K.; Büchler, J.; Spycher, R.; Dalmonte, P.; Volkin, D. B. Development of a Microflow Digital Imaging Assay to Characterize Protein Particulates during Storage of a High Concentration IgG1 Monoclonal Antibody Formulation J. Pharm. Sci. 2010, 99, 3343-3361 10.1002/jps.22123
    • (2010) J. Pharm. Sci. , vol.99 , pp. 3343-3361
    • Wuchner, K.1    Büchler, J.2    Spycher, R.3    Dalmonte, P.4    Volkin, D.B.5
  • 18
    • 77953291167 scopus 로고    scopus 로고
    • Critical Evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the Measurement of Nanoparticles and Protein Aggregates
    • Filipe, V.; Hawe, A.; Jiskoot, W. Critical Evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the Measurement of Nanoparticles and Protein Aggregates Pharm. Res. 2010, 27, 796-810 10.1007/s11095-010-0073-2
    • (2010) Pharm. Res. , vol.27 , pp. 796-810
    • Filipe, V.1    Hawe, A.2    Jiskoot, W.3
  • 19
    • 84926340393 scopus 로고    scopus 로고
    • Characterization of Submicron (0.1-1 ?m) Particles in Therapeutic Proteins by Nanoparticle Tracking Analysis
    • Vasudev, R.; Mathew, S.; Afonina, N. Characterization of Submicron (0.1-1 ?m) Particles in Therapeutic Proteins by Nanoparticle Tracking Analysis J. Pharm. Sci. 2015, 104, 1622-1631 10.1002/jps.24411
    • (2015) J. Pharm. Sci. , vol.104 , pp. 1622-1631
    • Vasudev, R.1    Mathew, S.2    Afonina, N.3
  • 20
    • 84905386771 scopus 로고    scopus 로고
    • The Fab Conformations in the Solution Structure of Human Immunoglobulin G4 (IgG4) Restrict Access to Its Fc Region: Implications for Functional Activity
    • Rayner, L. E.; Hui, G. K.; Gor, J.; Heenan, R. K.; Dalby, P. A.; Perkins, S. J. The Fab Conformations in the Solution Structure of Human Immunoglobulin G4 (IgG4) Restrict Access to Its Fc Region: Implications for Functional Activity J. Biol. Chem. 2014, 289, 20740-20756 10.1074/jbc.M114.572404
    • (2014) J. Biol. Chem. , vol.289 , pp. 20740-20756
    • Rayner, L.E.1    Hui, G.K.2    Gor, J.3    Heenan, R.K.4    Dalby, P.A.5    Perkins, S.J.6
  • 22
    • 84872490354 scopus 로고    scopus 로고
    • High-Throughput Melting-Temperature Analysis of a Monoclonal Antibody by Differential Scanning Fluorimetry in the Presence of Surfactants
    • Menzen, T.; Friess, W. High-Throughput Melting-Temperature Analysis of a Monoclonal Antibody by Differential Scanning Fluorimetry in the Presence of Surfactants J. Pharm. Sci. 2013, 102, 415-428 10.1002/jps.23405
    • (2013) J. Pharm. Sci. , vol.102 , pp. 415-428
    • Menzen, T.1    Friess, W.2
  • 23
    • 78650154417 scopus 로고    scopus 로고
    • Molecular Level Insights into Thermally Induced α-Chymotrypsinogen A Amyloid Aggregation Mechanism and Semiflexible Protofibril Morphology
    • Zhang, A.; Jordan, J. L.; Ivanova, M. I.; Weiss, W. F.; Roberts, C. J.; Fernandez, E. J. Molecular Level Insights into Thermally Induced α-Chymotrypsinogen A Amyloid Aggregation Mechanism and Semiflexible Protofibril Morphology Biochemistry 2010, 49, 10553-10564 10.1021/bi1014216
    • (2010) Biochemistry , vol.49 , pp. 10553-10564
    • Zhang, A.1    Jordan, J.L.2    Ivanova, M.I.3    Weiss, W.F.4    Roberts, C.J.5    Fernandez, E.J.6
  • 24
    • 79954531753 scopus 로고    scopus 로고
    • Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions: Part 1. Unfolding, Colloidal Interactions, and Formation of High-Molecular-Weight Aggregates
    • Brummitt, R. K.; Nesta, D. P.; Chang, L.; Chase, S. F.; Laue, T. M.; Roberts, C. J. Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions: Part 1. Unfolding, Colloidal Interactions, and Formation of High-Molecular-Weight Aggregates J. Pharm. Sci. 2011, 100, 2087-2103 10.1002/jps.22448
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 25
    • 84873886259 scopus 로고    scopus 로고
    • Aggregation of Anti-Streptavidin Immunoglobulin gamma-1 Involves Fab Unfolding and Competing Growth Pathways Mediated by pH and Salt Concentration
    • Kim, N.; Remmele, R. L.; Liu, D.; Razinkov, V. I.; Fernandez, E. J.; Roberts, C. J. Aggregation of Anti-Streptavidin Immunoglobulin gamma-1 Involves Fab Unfolding and Competing Growth Pathways Mediated by pH and Salt Concentration Biophys. Chem. 2013, 172, 26-36 10.1016/j.bpc.2012.12.004
    • (2013) Biophys. Chem. , vol.172 , pp. 26-36
    • Kim, N.1    Remmele, R.L.2    Liu, D.3    Razinkov, V.I.4    Fernandez, E.J.5    Roberts, C.J.6
  • 26
    • 84896086830 scopus 로고    scopus 로고
    • Competing Aggregation Pathways for Monoclonal Antibodies
    • Wu, H.; Kroe-Barrett, R.; Singh, S.; Robinson, A. S.; Roberts, C. J. Competing Aggregation Pathways for Monoclonal Antibodies FEBS Lett. 2014, 588, 936-941 10.1016/j.febslet.2014.01.051
    • (2014) FEBS Lett. , vol.588 , pp. 936-941
    • Wu, H.1    Kroe-Barrett, R.2    Singh, S.3    Robinson, A.S.4    Roberts, C.J.5
  • 27
    • 79954494833 scopus 로고    scopus 로고
    • Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions, Part 2: Nucleation and Growth Kinetics with Competing Growth Mechanisms
    • Brummitt, R. K.; Nesta, D. P.; Chang, L.; Kroetsch, A. M.; Roberts, C. J. Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions, Part 2: Nucleation and Growth Kinetics with Competing Growth Mechanisms J. Pharm. Sci. 2011, 100, 2104-2119 10.1002/jps.22447
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2104-2119
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Kroetsch, A.M.4    Roberts, C.J.5
  • 28
    • 84863981137 scopus 로고    scopus 로고
    • From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
    • Cohen, S. I. A.; Vendruscolo, M.; Dobson, C. M.; Knowles, T. P. J. From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation J. Mol. Biol. 2012, 421, 160-171 10.1016/j.jmb.2012.02.031
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 29
    • 84928963134 scopus 로고    scopus 로고
    • Specific-Ion Effects on the Aggregation Mechanisms and Protein-Protein Interactions for Anti-Streptavidin Immunoglobulin Gamma-1
    • Barnett, G. V.; Razinkov, V. I.; Kerwin, B. A.; Laue, T. M.; Woodka, A. H.; Butler, P. D.; Perevozchikova, T.; Roberts, C. J. Specific-Ion Effects on the Aggregation Mechanisms and Protein-Protein Interactions for Anti-Streptavidin Immunoglobulin Gamma-1 J. Phys. Chem. B 2015, 119, 5793-5804 10.1021/acs.jpcb.5b01881
    • (2015) J. Phys. Chem. B , vol.119 , pp. 5793-5804
    • Barnett, G.V.1    Razinkov, V.I.2    Kerwin, B.A.3    Laue, T.M.4    Woodka, A.H.5    Butler, P.D.6    Perevozchikova, T.7    Roberts, C.J.8
  • 32
    • 68749118103 scopus 로고    scopus 로고
    • Structural Properties of Monoclonal Antibody Aggregates Induced by Freeze-thawing and Thermal Stress
    • Hawe, A.; Kasper, J. C.; Friess, W.; Jiskoot, W. Structural Properties of Monoclonal Antibody Aggregates Induced by Freeze-thawing and Thermal Stress Eur. J. Pharm. Sci. 2009, 38, 79-87 10.1016/j.ejps.2009.06.001
    • (2009) Eur. J. Pharm. Sci. , vol.38 , pp. 79-87
    • Hawe, A.1    Kasper, J.C.2    Friess, W.3    Jiskoot, W.4
  • 34
    • 79960128166 scopus 로고    scopus 로고
    • Classification and Characterization of Therapeutic Antibody Aggregates
    • Joubert, M. K.; Luo, Q.; Nashed-Samuel, Y.; Wypych, J.; Narhi, L. O. Classification and Characterization of Therapeutic Antibody Aggregates J. Biol. Chem. 2011, 286, 25118-25133 10.1074/jbc.M110.160457
    • (2011) J. Biol. Chem. , vol.286 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 35
    • 84862876623 scopus 로고    scopus 로고
    • Native-State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies
    • Banks, D. D.; Latypov, R. F.; Ketchem, R. R.; Woodard, J.; Scavezze, J. L.; Siska, C. C.; Razinkov, V. I. Native-State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies J. Pharm. Sci. 2012, 101, 2720-2732 10.1002/jps.23219
    • (2012) J. Pharm. Sci. , vol.101 , pp. 2720-2732
    • Banks, D.D.1    Latypov, R.F.2    Ketchem, R.R.3    Woodard, J.4    Scavezze, J.L.5    Siska, C.C.6    Razinkov, V.I.7
  • 36
    • 84868128716 scopus 로고    scopus 로고
    • Aggregation-Prone Near-Native Intermediate Formation during Unfolding of a Structurally Similar Nonlenticular β?-Crystallin Domain
    • Rajanikanth, V.; Srivastava, S. S.; Singh, A. K.; Rajyalakshmi, M.; Chandra, K.; Aravind, P.; Sankaranarayanan, R.; Sharma, Y. Aggregation-Prone Near-Native Intermediate Formation during Unfolding of a Structurally Similar Nonlenticular β?-Crystallin Domain Biochemistry 2012, 51, 8502-8513 10.1021/bi300844u
    • (2012) Biochemistry , vol.51 , pp. 8502-8513
    • Rajanikanth, V.1    Srivastava, S.S.2    Singh, A.K.3    Rajyalakshmi, M.4    Chandra, K.5    Aravind, P.6    Sankaranarayanan, R.7    Sharma, Y.8
  • 37
    • 84861872576 scopus 로고    scopus 로고
    • Characterizing Intermolecular Interactions That Initiate Native-Like Protein Aggregation
    • Bemporad, F.; De Simone, A.; Chiti, F.; Dobson, C. M. Characterizing Intermolecular Interactions That Initiate Native-Like Protein Aggregation Biophys. J. 2012, 102, 2595-2604 10.1016/j.bpj.2012.03.057
    • (2012) Biophys. J. , vol.102 , pp. 2595-2604
    • Bemporad, F.1    De Simone, A.2    Chiti, F.3    Dobson, C.M.4
  • 38
    • 0001591464 scopus 로고
    • Use of the Glass Electrode in Deuterium Oxide and the Relation between the Standardized pD (paD) Scale and the Operational pH in Heavy Water
    • Covington, A. K.; Paabo, M.; Robinson, R. A.; Bates, R. G. Use of the Glass Electrode in Deuterium Oxide and the Relation between the Standardized pD (paD) Scale and the Operational pH in Heavy Water Anal. Chem. 1968, 40, 700-706 10.1021/ac60260a013
    • (1968) Anal. Chem. , vol.40 , pp. 700-706
    • Covington, A.K.1    Paabo, M.2    Robinson, R.A.3    Bates, R.G.4
  • 41
    • 74049123780 scopus 로고    scopus 로고
    • Multi-Variate Approach to Global Protein Aggregation Behavior and Kinetics: Effects of pH, NaCl, and Temperature for Alpha-Chymotrypsinogen A
    • Li, Y.; Ogunnaike, B. A.; Roberts, C. J. Multi-Variate Approach to Global Protein Aggregation Behavior and Kinetics: Effects of pH, NaCl, and Temperature for Alpha-Chymotrypsinogen A J. Pharm. Sci. 2010, 99, 645-662 10.1002/jps.21869
    • (2010) J. Pharm. Sci. , vol.99 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 42
    • 84934441181 scopus 로고    scopus 로고
    • Ultraviolet Absorption Spectroscopy of Peptides-Springer
    • Humana Press
    • Ultraviolet Absorption Spectroscopy of Peptides-Springer. In Methods in Molecular Biology; Nixon, A. E., Ed.; Humana Press, 2014.
    • (2014) Methods in Molecular Biology
    • Nixon, A.E.1
  • 43
    • 0038161224 scopus 로고    scopus 로고
    • Revisiting the Method of Cumulants for the Analysis of Dynamic Light-Scattering Data
    • Frisken, B. J. Revisiting the Method of Cumulants for the Analysis of Dynamic Light-Scattering Data Appl. Opt. 2001, 40, 4087-4091 10.1364/AO.40.004087
    • (2001) Appl. Opt. , vol.40 , pp. 4087-4091
    • Frisken, B.J.1
  • 44
    • 36849103950 scopus 로고
    • Analysis of Macromolecular Polydispersity in Intensity Correlation Spectroscopy: The Method of Cumulants
    • Koppel, D. E. Analysis of Macromolecular Polydispersity in Intensity Correlation Spectroscopy: The Method of Cumulants J. Chem. Phys. 1972, 57, 4814-4820 10.1063/1.1678153
    • (1972) J. Chem. Phys. , vol.57 , pp. 4814-4820
    • Koppel, D.E.1
  • 45
    • 84919752783 scopus 로고    scopus 로고
    • Combined Dynamic Light Scattering and Raman Spectroscopy Approach for Characterizing the Aggregation of Therapeutic Proteins
    • Lewis, E. N.; Qi, W.; Kidder, L. H.; Amin, S.; Kenyon, S. M.; Blake, S. Combined Dynamic Light Scattering and Raman Spectroscopy Approach for Characterizing the Aggregation of Therapeutic Proteins Molecules 2014, 19, 20888-20905 10.3390/molecules191220888
    • (2014) Molecules , vol.19 , pp. 20888-20905
    • Lewis, E.N.1    Qi, W.2    Kidder, L.H.3    Amin, S.4    Kenyon, S.M.5    Blake, S.6
  • 46
    • 84921021627 scopus 로고    scopus 로고
    • Concomitant Raman Spectroscopy and Dynamic Light Scattering for Characterization of Therapeutic Proteins at High Concentrations
    • Zhou, C.; Qi, W.; Neil Lewis, E.; Carpenter, J. F. Concomitant Raman Spectroscopy and Dynamic Light Scattering for Characterization of Therapeutic Proteins at High Concentrations Anal. Biochem. 2015, 472, 7-20 10.1016/j.ab.2014.11.016
    • (2015) Anal. Biochem. , vol.472 , pp. 7-20
    • Zhou, C.1    Qi, W.2    Neil Lewis, E.3    Carpenter, J.F.4
  • 47
    • 84919683934 scopus 로고    scopus 로고
    • A Novel Combination of DLS-Optical Microrheology and Low Frequency Raman Spectroscopy to Reveal Underlying Biopolymer Self-Assembly and Gelation Mechanisms
    • Amin, S.; Blake, S.; Kenyon, S. M.; Kennel, R. C.; Lewis, E. N. A Novel Combination of DLS-Optical Microrheology and Low Frequency Raman Spectroscopy to Reveal Underlying Biopolymer Self-Assembly and Gelation Mechanisms J. Chem. Phys. 2014, 141, 234201 10.1063/1.4903785
    • (2014) J. Chem. Phys. , vol.141 , pp. 234201
    • Amin, S.1    Blake, S.2    Kenyon, S.M.3    Kennel, R.C.4    Lewis, E.N.5
  • 48
    • 33751206216 scopus 로고    scopus 로고
    • Reduction and Analysis of SANS and USANS Data Using IGOR Pro
    • Kline, S. R. Reduction and Analysis of SANS and USANS Data Using IGOR Pro J. Appl. Crystallogr. 2006, 39, 895-900 10.1107/S0021889806035059
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 895-900
    • Kline, S.R.1
  • 50
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics. 2. Competing Growth via Condensation and Chain Polymerization
    • Li, Y.; Roberts, C. J. Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics. 2. Competing Growth via Condensation and Chain Polymerization J. Phys. Chem. B 2009, 113, 7020-7032 10.1021/jp8083088
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 51
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative Protein Polymers: Structure, Morphology, and Relation to Nucleation and Growth
    • Weiss, W. F.; Hodgdon, T. K.; Kaler, E. W.; Lenhoff, A. M.; Roberts, C. J. Nonnative Protein Polymers: Structure, Morphology, and Relation to Nucleation and Growth Biophys. J. 2007, 93, 4392-4403 10.1529/biophysj.107.112102
    • (2007) Biophys. J. , vol.93 , pp. 4392-4403
    • Weiss, W.F.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 52
    • 84880541690 scopus 로고    scopus 로고
    • Isolation of a Highly Reactive β-Sheet-Rich Intermediate of Lysozyme in a Solvent-Free Liquid Phase
    • Brogan, A. P. S.; Sharma, K. P.; Perriman, A. W.; Mann, S. Isolation of a Highly Reactive β-Sheet-Rich Intermediate of Lysozyme in a Solvent-Free Liquid Phase J. Phys. Chem. B 2013, 117, 8400-8407 10.1021/jp4041524
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8400-8407
    • Brogan, A.P.S.1    Sharma, K.P.2    Perriman, A.W.3    Mann, S.4
  • 53
    • 84878893050 scopus 로고    scopus 로고
    • Aggregation Mechanism of an IgG2 and Two IgG1 Monoclonal Antibodies at Low pH: From Oligomers to Larger Aggregates
    • Arosio, P.; Rima, S.; Morbidelli, M. Aggregation Mechanism of an IgG2 and Two IgG1 Monoclonal Antibodies at Low pH: From Oligomers to Larger Aggregates Pharm. Res. 2013, 30, 641-654 10.1007/s11095-012-0885-3
    • (2013) Pharm. Res. , vol.30 , pp. 641-654
    • Arosio, P.1    Rima, S.2    Morbidelli, M.3
  • 54
    • 33749318250 scopus 로고    scopus 로고
    • Probing Protein Structure and Dynamics by Second-Derivative Ultraviolet Absorption Analysis of Cation-? Interactions
    • Lucas, L. H.; Ersoy, B. A.; Kueltzo, L. A.; Joshi, S. B.; Brandau, D. T.; Thyagarajapuram, N.; Peek, L. J.; Middaugh, C. R. Probing Protein Structure and Dynamics by Second-Derivative Ultraviolet Absorption Analysis of Cation-? Interactions Protein Sci. 2006, 15, 2228-2243 10.1110/ps.062133706
    • (2006) Protein Sci. , vol.15 , pp. 2228-2243
    • Lucas, L.H.1    Ersoy, B.A.2    Kueltzo, L.A.3    Joshi, S.B.4    Brandau, D.T.5    Thyagarajapuram, N.6    Peek, L.J.7    Middaugh, C.R.8
  • 55
    • 84870709849 scopus 로고    scopus 로고
    • Application of Second-Derivative Fluorescence Spectroscopy to Monitor Subtle Changes in a Monoclonal Antibody Structure
    • Abbas, S. A.; Gaspar, G.; Sharma, V. K.; Patapoff, T. W.; Kalonia, D. S. Application of Second-Derivative Fluorescence Spectroscopy to Monitor Subtle Changes in a Monoclonal Antibody Structure J. Pharm. Sci. 2013, 102 (1) 52-61 10.1002/jps.23354
    • (2013) J. Pharm. Sci. , vol.102 , Issue.1 , pp. 52-61
    • Abbas, S.A.1    Gaspar, G.2    Sharma, V.K.3    Patapoff, T.W.4    Kalonia, D.S.5
  • 56
    • 36849073223 scopus 로고    scopus 로고
    • Raman Spectroscopy of Protein Pharmaceuticals
    • Wen, Z.-Q. Raman Spectroscopy of Protein Pharmaceuticals J. Pharm. Sci. 2007, 96, 2861-2878 10.1002/jps.20895
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2861-2878
    • Wen, Z.-Q.1
  • 57
    • 18444419164 scopus 로고    scopus 로고
    • Raman Spectroscopy of Proteins: From Peptides to Large Assemblies
    • Tuma, R. Raman Spectroscopy of Proteins: From Peptides to Large Assemblies J. Raman Spectrosc. 2005, 36, 307-319 10.1002/jrs.1323
    • (2005) J. Raman Spectrosc. , vol.36 , pp. 307-319
    • Tuma, R.1
  • 58
    • 0029753787 scopus 로고    scopus 로고
    • Theory, Design, and Characterization of a Microdialysis Flow Cell for Raman Spectroscopy
    • Tuma, R.; Thomas, G. J., Jr Theory, Design, and Characterization of a Microdialysis Flow Cell for Raman Spectroscopy Biophys. J. 1996, 71, 3454 10.1016/S0006-3495(96)79541-3
    • (1996) Biophys. J. , vol.71 , pp. 3454
    • Tuma, R.1    Thomas, G.J.2
  • 59
    • 0032544102 scopus 로고    scopus 로고
    • Mechanism of Capsid Maturation in a Double-Stranded DNA Virus
    • Tuma, R.; Prevelige, P. E.; Thomas, G. J. Mechanism of Capsid Maturation in a Double-Stranded DNA Virus Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 9885-9890 10.1073/pnas.95.17.9885
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9885-9890
    • Tuma, R.1    Prevelige, P.E.2    Thomas, G.J.3
  • 60
    • 0014972343 scopus 로고
    • Density and Viscosity of Deuterium Oxide Solutions from 5-70.deg
    • Millero, F. J.; Dexter, R.; Hoff, E. Density and Viscosity of Deuterium Oxide Solutions from 5-70.deg J. Chem. Eng. Data 1971, 16, 85-87 10.1021/je60048a006
    • (1971) J. Chem. Eng. Data , vol.16 , pp. 85-87
    • Millero, F.J.1    Dexter, R.2    Hoff, E.3
  • 62
    • 84939217619 scopus 로고    scopus 로고
    • Aggregate Structure, Morphology and the Effect of Aggregation Mechanisms on Viscosity at Elevated Protein Concentrations
    • Barnett, G. V.; Qi, W.; Amin, S.; Neil Lewis, E.; Roberts, C. J. Aggregate Structure, Morphology and the Effect of Aggregation Mechanisms on Viscosity at Elevated Protein Concentrations Biophys. Chem. 2015, 207, 21-29 10.1016/j.bpc.2015.07.002
    • (2015) Biophys. Chem. , vol.207 , pp. 21-29
    • Barnett, G.V.1    Qi, W.2    Amin, S.3    Neil Lewis, E.4    Roberts, C.J.5
  • 63
    • 84881588643 scopus 로고    scopus 로고
    • A Systematic Multitechnique Approach for Detection and Characterization of Reversible Self-Association during Formulation Development of Therapeutic Antibodies
    • Esfandiary, R.; Hayes, D. B.; Parupudi, A.; Casas-finet, J.; Bai, S.; Samra, H. S.; Shah, A. U.; Sathish, H. A. A Systematic Multitechnique Approach for Detection and Characterization of Reversible Self-Association during Formulation Development of Therapeutic Antibodies J. Pharm. Sci. 2013, 102, 62-72 10.1002/jps.23369
    • (2013) J. Pharm. Sci. , vol.102 , pp. 62-72
    • Esfandiary, R.1    Hayes, D.B.2    Parupudi, A.3    Casas-Finet, J.4    Bai, S.5    Samra, H.S.6    Shah, A.U.7    Sathish, H.A.8
  • 64
    • 0031119765 scopus 로고    scopus 로고
    • Angular Dependence in Static and Dynamic Light Scattering from Randomly Branched Systems
    • Trappe, V.; Bauer, J.; Weissmüller, M.; Burchard, W. Angular Dependence in Static and Dynamic Light Scattering from Randomly Branched Systems Macromolecules 1997, 30, 2365-2372 10.1021/ma961728w
    • (1997) Macromolecules , vol.30 , pp. 2365-2372
    • Trappe, V.1    Bauer, J.2    Weissmüller, M.3    Burchard, W.4
  • 65
    • 1642633079 scopus 로고    scopus 로고
    • Solution Properties of Branched Macromolecules
    • Springer: New York
    • Burchard, W. Solution Properties of Branched Macromolecules. In Branched polymers II; Springer: New York, 1999; pp 113-194.
    • (1999) Branched Polymers II , pp. 113-194
    • Burchard, W.1
  • 66
    • 84902001346 scopus 로고    scopus 로고
    • Protein-Protein Interactions in Dilute to Concentrated Solutions: α-Chymotrypsinogen in Acidic Conditions
    • Blanco, M. A.; Perevozchikova, T.; Martorana, V.; Manno, M.; Roberts, C. J. Protein-Protein Interactions in Dilute to Concentrated Solutions: α-Chymotrypsinogen in Acidic Conditions J. Phys. Chem. B 2014, 118, 5817-5831 10.1021/jp412301h
    • (2014) J. Phys. Chem. B , vol.118 , pp. 5817-5831
    • Blanco, M.A.1    Perevozchikova, T.2    Martorana, V.3    Manno, M.4    Roberts, C.J.5
  • 67
    • 84857132923 scopus 로고    scopus 로고
    • How Random Are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective
    • Receveur-Bréchot, V.; Durand, D. How Random Are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective Curr. Protein Pept. Sci. 2012, 13, 55 10.2174/138920312799277901
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 55
    • Receveur-Bréchot, V.1    Durand, D.2
  • 68
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding
    • Andrews, J. M.; Roberts, C. J. A Lumry-Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding J. Phys. Chem. B 2007, 111, 7897-7913 10.1021/jp070212j
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 69
    • 4243632346 scopus 로고
    • Diffusion-Limited Aggregation, a Kinetic Critical Phenomenon
    • Witten, T. A.; Sander, L. M. Diffusion-Limited Aggregation, a Kinetic Critical Phenomenon Phys. Rev. Lett. 1981, 47, 1400-1403 10.1103/PhysRevLett.47.1400
    • (1981) Phys. Rev. Lett. , vol.47 , pp. 1400-1403
    • Witten, T.A.1    Sander, L.M.2
  • 71
    • 0019888281 scopus 로고
    • The Stabilization of Proteins by Sucrose
    • Lee, J. C.; Timasheff, S. N. The Stabilization of Proteins by Sucrose J. Biol. Chem. 1981, 256, 7193-7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 72
    • 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.; Carpenter, J. F. Preferential Exclusion of Sucrose from Recombinant Interleukin-1 Receptor Antagonist: Role in Restricted Conformational Mobility and Compaction of Native State Proc. Natl. Acad. Sci. U. S. A. 1997, 94, 11917-11922 10.1073/pnas.94.22.11917
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 73
    • 57049105810 scopus 로고    scopus 로고
    • Structural Thermodynamics of Protein Preferential Solvation: Osmolyte Solvation of Proteins, Amino Acids, and Peptides
    • Auton, M.; Bolen, D. W.; Rösgen, J. Structural Thermodynamics of Protein Preferential Solvation: Osmolyte Solvation of Proteins, Amino Acids, and Peptides Proteins: Struct., Funct., Genet. 2008, 73, 802-813 10.1002/prot.22103
    • (2008) Proteins: Struct., Funct., Genet. , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rösgen, J.3
  • 74
    • 84926662608 scopus 로고    scopus 로고
    • Effects of Sucrose and Benzyl Alcohol on GCSF Conformational Dynamics Revealed by Hydrogen Deuterium Exchange Mass Spectrometry
    • Zhang, J.; Banks, D. D.; He, F.; Treuheit, M. J.; Becker, G. W. Effects of Sucrose and Benzyl Alcohol on GCSF Conformational Dynamics Revealed by Hydrogen Deuterium Exchange Mass Spectrometry J. Pharm. Sci. 2015, 104, 1592-1600 10.1002/jps.24384
    • (2015) J. Pharm. Sci. , vol.104 , pp. 1592-1600
    • Zhang, J.1    Banks, D.D.2    He, F.3    Treuheit, M.J.4    Becker, G.W.5


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