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Volumn 29, Issue 14, 2013, Pages 4584-4593

PH-dependent aggregation and disaggregation of native β-lactoglobulin in low salt

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATE STRUCTURES; BOVINE SERUM ALBUMINS; CHARGE FLUCTUATIONS; ISO-ELECTRIC POINTS; KINETIC MEASUREMENT; LOCALIZED CHARGE; STATIC LIGHT SCATTERING; UNIFORM REDUCTION;

EID: 84875980546     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la400258r     Document Type: Article
Times cited : (59)

References (60)
  • 1
    • 84862693132 scopus 로고    scopus 로고
    • Population Balance Modeling of Antibodies Aggregation Kinetics
    • Arosio, P.; Rima, S.; Lattuada, M.; Morbidelli, M. Population Balance Modeling of Antibodies Aggregation Kinetics J. Phys. Chem. B 2012, 116, 7066-7075
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7066-7075
    • Arosio, P.1    Rima, S.2    Lattuada, M.3    Morbidelli, M.4
  • 2
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry-Eyring Models and Implications for Predicting Protein Shelf Life
    • Roberts, C. J. Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry-Eyring Models and Implications for Predicting Protein Shelf Life J. Phys. Chem. B 2003, 107, 1194-1207
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1194-1207
    • Roberts, C.J.1
  • 4
    • 35648945914 scopus 로고    scopus 로고
    • Protein Aggregation Processes: In Search of the Mechanism
    • Frieden, C. Protein Aggregation Processes: In Search of the Mechanism Protein Sci. 2007, 16, 2334-2344
    • (2007) Protein Sci. , vol.16 , pp. 2334-2344
    • Frieden, C.1
  • 5
    • 0031932169 scopus 로고    scopus 로고
    • Protein Aggregation: Folding Aggregates, Inclusion Bodies and Amyloid
    • Fink, A. L. Protein Aggregation: Folding Aggregates, Inclusion Bodies and Amyloid Fold. Des. 1998, 3, R9-R23
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 6
    • 77951977004 scopus 로고    scopus 로고
    • Protein Kinetic Stability
    • Sanchez-Ruiz, J. M. Protein Kinetic Stability Biophys. Chem. 2010, 148, 1-15
    • (2010) Biophys. Chem. , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 7
    • 79961023076 scopus 로고    scopus 로고
    • β-Lactoglobulin and WPI Aggregates: Formation, Structure and Applications
    • Nicolai, T.; Britten, M.; Schmitt, C. β-Lactoglobulin and WPI Aggregates: Formation, Structure and Applications Food Hydrocolloids 2011, 25, 1945-1962
    • (2011) Food Hydrocolloids , vol.25 , pp. 1945-1962
    • Nicolai, T.1    Britten, M.2    Schmitt, C.3
  • 9
    • 0030961726 scopus 로고    scopus 로고
    • Entropy in Protein Folding and in Protein-Protein Interactions
    • Brady, G. P.; Sharp, K. A. Entropy in Protein Folding and in Protein-Protein Interactions Curr. Opin. Struct. Biol. 1997, 7, 215-221
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 215-221
    • Brady, G.P.1    Sharp, K.A.2
  • 10
    • 0038071858 scopus 로고    scopus 로고
    • Ionic Strength Dependence of Protein-Polyelectrolyte Interactions
    • Seyrek, E.; Dubin, P. L.; Tribet, C.; Gamble, E. A. Ionic Strength Dependence of Protein-Polyelectrolyte Interactions Biomacromolecules 2003, 4, 273-282
    • (2003) Biomacromolecules , vol.4 , pp. 273-282
    • Seyrek, E.1    Dubin, P.L.2    Tribet, C.3    Gamble, E.A.4
  • 11
    • 0027113235 scopus 로고
    • Effects of Protein Charge Heterogeneity in Protein-Polyelectrolyte Complexation
    • Park, J. M.; Muhoberac, B. B.; Dubin, P. L.; Xia, J. L. Effects of Protein Charge Heterogeneity in Protein-Polyelectrolyte Complexation Macromolecules 1992, 25, 290-295
    • (1992) Macromolecules , vol.25 , pp. 290-295
    • Park, J.M.1    Muhoberac, B.B.2    Dubin, P.L.3    Xia, J.L.4
  • 12
    • 0034888148 scopus 로고    scopus 로고
    • Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site
    • Grymonpre, K. R.; Staggemeier, B. A.; Dubin, P. L.; Mattison, K. W. Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site Biomacromolecules 2001, 2, 422-429
    • (2001) Biomacromolecules , vol.2 , pp. 422-429
    • Grymonpre, K.R.1    Staggemeier, B.A.2    Dubin, P.L.3    Mattison, K.W.4
  • 13
    • 84856985857 scopus 로고    scopus 로고
    • Stability of White Wine Proteins: Combined Effect of pH, Ionic Strength, and Temperature on Their Aggregation
    • Dufrechou, M.; Poncet-Legrand, C.; Sauvage, F. X.; Vernhet, A. Stability of White Wine Proteins: Combined Effect of pH, Ionic Strength, and Temperature on Their Aggregation J. Agric. Food Chem. 2012, 60, 1308-1319
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 1308-1319
    • Dufrechou, M.1    Poncet-Legrand, C.2    Sauvage, F.X.3    Vernhet, A.4
  • 14
    • 33644751068 scopus 로고    scopus 로고
    • What Is the Role of Thermodynamics on Protein Stability?
    • Gummadi, S. N. What Is the Role of Thermodynamics on Protein Stability? Biotechnol. Bioprocess Eng. 2003, 8, 9-18
    • (2003) Biotechnol. Bioprocess Eng. , vol.8 , pp. 9-18
    • Gummadi, S.N.1
  • 15
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, Electrostatically Assisted Association of Proteins
    • Schreiber, G.; Fersht, A. R. Rapid, Electrostatically Assisted Association of Proteins Nat. Struct. Biol. 1996, 3, 427-431
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 16
    • 0033605858 scopus 로고    scopus 로고
    • Predicting the Rate Enhancement of Protein Complex Formation from the Electrostatic Energy of Interaction
    • Selzer, T.; Schreiber, G. Predicting the Rate Enhancement of Protein Complex Formation from the Electrostatic Energy of Interaction J. Mol. Biol. 1999, 287, 409-419
    • (1999) J. Mol. Biol. , vol.287 , pp. 409-419
    • Selzer, T.1    Schreiber, G.2
  • 17
    • 17844405882 scopus 로고    scopus 로고
    • A Consistent Experimental and Modeling Approach to Light-Scattering Studies of Protein-Protein Interactions in Solution
    • Asthagiri, D.; Paliwal, A.; Abras, D.; Lenhoff, A. M.; Paulaitis, M. E. A Consistent Experimental and Modeling Approach to Light-Scattering Studies of Protein-Protein Interactions in Solution Biophys. J. 2005, 88, 3300-3309
    • (2005) Biophys. J. , vol.88 , pp. 3300-3309
    • Asthagiri, D.1    Paliwal, A.2    Abras, D.3    Lenhoff, A.M.4    Paulaitis, M.E.5
  • 18
    • 27144472219 scopus 로고    scopus 로고
    • Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering
    • Liu, Y.; Fratini, E.; Baglioni, P.; Chen, W. R.; Chen, S. H. Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering Phys. Rev. Lett. 2005, 95, 118402
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 118402
    • Liu, Y.1    Fratini, E.2    Baglioni, P.3    Chen, W.R.4    Chen, S.H.5
  • 20
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of Protein Aggregation Kinetics
    • Ferrone, F. Analysis of Protein Aggregation Kinetics Methods Enzymol. 1999, 309, 256-274
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 24
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically Driven Protein Aggregation: Beta-Lactoglobulin at Low Ionic Strength
    • Majhi, P. R.; Ganta, R. R.; Vanam, R. P.; Seyrek, E.; Giger, K.; Dubin, P. L. Electrostatically Driven Protein Aggregation: beta-Lactoglobulin at Low Ionic Strength Langmuir 2006, 22, 9150-9159
    • (2006) Langmuir , vol.22 , pp. 9150-9159
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 25
    • 84861111636 scopus 로고    scopus 로고
    • Effect of Heparin on Protein Aggregation: Inhibition versus Promotion
    • Xu, Y.; Seeman, D.; Yan, Y. F.; Sun, L. H.; Post, J.; Dubin, P. L. Effect of Heparin on Protein Aggregation: Inhibition versus Promotion Biomacromolecules 2012, 13, 1642-1651
    • (2012) Biomacromolecules , vol.13 , pp. 1642-1651
    • Xu, Y.1    Seeman, D.2    Yan, Y.F.3    Sun, L.H.4    Post, J.5    Dubin, P.L.6
  • 26
    • 84862908149 scopus 로고    scopus 로고
    • Multimerization and Aggregation of Native-State Insulin: Effect of Zinc
    • Xu, Y. S.; Yan, Y. F.; Seeman, D.; Sun, L. H.; Dubin, P. L. Multimerization and Aggregation of Native-State Insulin: Effect of Zinc Langmuir 2012, 28, 579-586
    • (2012) Langmuir , vol.28 , pp. 579-586
    • Xu, Y.S.1    Yan, Y.F.2    Seeman, D.3    Sun, L.H.4    Dubin, P.L.5
  • 28
    • 34247360046 scopus 로고    scopus 로고
    • Whey Protein Soluble Aggregates from Heating with NaCl: Physicochemical, Interfacial, and Foaming Properties
    • Schmitt, C.; Bovay, C.; Rouvet, M.; Shojaei-Rami, S.; Kolodziejczyk, E. Whey Protein Soluble Aggregates from Heating with NaCl: Physicochemical, Interfacial, and Foaming Properties Langmuir 2007, 23, 4155-4166
    • (2007) Langmuir , vol.23 , pp. 4155-4166
    • Schmitt, C.1    Bovay, C.2    Rouvet, M.3    Shojaei-Rami, S.4    Kolodziejczyk, E.5
  • 29
    • 0031758168 scopus 로고    scopus 로고
    • Protein Modification by Thermal Processing
    • Davis, P. J.; Williams, S. C. Protein Modification by Thermal Processing Allergy 1998, 53, 102-105
    • (1998) Allergy , vol.53 , pp. 102-105
    • Davis, P.J.1    Williams, S.C.2
  • 30
    • 1542286920 scopus 로고    scopus 로고
    • Modification of IgE Binding during Heat Processing of the Cow's Milk Allergen β-Lactoglobulin
    • Ehn, B. M.; Ekstrand, B.; Bengtsson, U.; Ahlstedt, S. Modification of IgE Binding during Heat Processing of the Cow's Milk Allergen β-Lactoglobulin J. Agric. Food Chem. 2004, 52, 1398-1403
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1398-1403
    • Ehn, B.M.1    Ekstrand, B.2    Bengtsson, U.3    Ahlstedt, S.4
  • 31
    • 0036784667 scopus 로고    scopus 로고
    • A Kinetic Study of beta-Lactoglobulin Amyloid Fibril Formation Promoted by Urea
    • Hamada, D.; Dobson, C. M. A Kinetic Study of beta-Lactoglobulin Amyloid Fibril Formation Promoted by Urea Protein Sci. 2002, 11, 2417-2426
    • (2002) Protein Sci. , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 32
    • 68949142908 scopus 로고    scopus 로고
    • Amyloid Fibril-Like Structure Underlies the Aggregate Structure across the pH Range for beta-Lactoglobulin
    • Krebs, M. R. H.; Devlin, G. L.; Donald, A. M. Amyloid Fibril-Like Structure Underlies the Aggregate Structure across the pH Range for beta-Lactoglobulin Biophys. J. 2009, 96, 5013-5019
    • (2009) Biophys. J. , vol.96 , pp. 5013-5019
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 33
    • 33750361540 scopus 로고    scopus 로고
    • A Century-Old Debate on Protein Aggregation and Neurodegeneration Enters the Clinic
    • Lansbury, P. T.; Lashuel, H. A. A Century-Old Debate on Protein Aggregation and Neurodegeneration Enters the Clinic Nature 2006, 443, 774-779
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 34
    • 0000295322 scopus 로고    scopus 로고
    • Kinetics of Heat-Induced Aggregation of β-Lactoglobulin
    • Verheul, M.; Roefs, S.; de Kruif, K. G. Kinetics of Heat-Induced Aggregation of β-Lactoglobulin J. Agric. Food Chem. 1998, 46, 896-903
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 896-903
    • Verheul, M.1    Roefs, S.2    De Kruif, K.G.3
  • 35
    • 0001029710 scopus 로고    scopus 로고
    • Growth and Structure of Aggregates of Heat-Denatured β-Lactoglobulin
    • Le Bon, C.; Nicolai, T.; Durand, D. Growth and Structure of Aggregates of Heat-Denatured β-Lactoglobulin Int. J. Food Sci. Technol. 1999, 34, 451-465
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 451-465
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 37
    • 0014198603 scopus 로고
    • Effect of pH on β-Lactoglobulins
    • McKenzie, H. A.; Sawyer, W. H. Effect of pH on β-Lactoglobulins Nature 1967, 214, 1101-1104
    • (1967) Nature , vol.214 , pp. 1101-1104
    • McKenzie, H.A.1    Sawyer, W.H.2
  • 38
    • 0032004945 scopus 로고    scopus 로고
    • Effects of pH and Salt Environment on the Association of β-Lactoglobulin Revealed by Intrinsic Fluorescence Studies
    • Renard, D.; Lefebvre, J.; Griffin, M. C. A.; Griffin, W. G. Effects of pH and Salt Environment on the Association of β-Lactoglobulin Revealed by Intrinsic Fluorescence Studies Int. J. Biol. Macromol. 1998, 22, 41-49
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 41-49
    • Renard, D.1    Lefebvre, J.2    Griffin, M.C.A.3    Griffin, W.G.4
  • 42
    • 0042532737 scopus 로고    scopus 로고
    • Protein Self-association in Solution: The Bovine β-Lactoglobulin Dimer and Octamer
    • Gottschalk, M.; Nilsson, H.; Roos, H.; Halle, B. Protein Self-association in Solution: The Bovine β-Lactoglobulin Dimer and Octamer Protein Sci. 2003, 12, 2404-2411
    • (2003) Protein Sci. , vol.12 , pp. 2404-2411
    • Gottschalk, M.1    Nilsson, H.2    Roos, H.3    Halle, B.4
  • 43
    • 0000819133 scopus 로고
    • Molecular Interactions in β-Lactoglobulin. 3. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.2
    • Townend, R.; Timasheff, S. N. Molecular Interactions in β-Lactoglobulin. 3. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.2 J. Am. Chem. Soc. 1960, 82, 3168-3174
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3168-3174
    • Townend, R.1    Timasheff, S.N.2
  • 44
    • 0000819131 scopus 로고
    • Molecular Interactions in β-Lactoglobulin. 2. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin below Its Isoelectric Point
    • Townend, R.; Winterbottom, R. J.; Timasheff, S. N. Molecular Interactions in β-Lactoglobulin. 2. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin Below Its Isoelectric Point J. Am. Chem. Soc. 1960, 82, 3161-3168
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3161-3168
    • Townend, R.1    Winterbottom, R.J.2    Timasheff, S.N.3
  • 45
    • 0000678430 scopus 로고
    • Structure of β-Lactoglobulin Tetramer
    • Timasheff, S. N.; Townend, R. Structure of β-Lactoglobulin Tetramer Nature 1964, 203, 517-519
    • (1964) Nature , vol.203 , pp. 517-519
    • Timasheff, S.N.1    Townend, R.2
  • 46
    • 33947335672 scopus 로고
    • Molecular Interactions in β-Lactoglobulin. X. Stoichiometry of β-Lactoglobulin Mixed Tetramerization
    • Kumosins, T. F.; Timashef, S. N. Molecular Interactions in β-Lactoglobulin. X. Stoichiometry of β-Lactoglobulin Mixed Tetramerization J. Am. Chem. Soc. 1966, 88, 5635-5642
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 5635-5642
    • Kumosins, T.F.1    Timashef, S.N.2
  • 47
    • 0036462040 scopus 로고    scopus 로고
    • Transient Clustering in a Protein Solution
    • Piazza, R.; Iacopini, S. Transient Clustering in a Protein Solution Eur. Phys. J. E 2002, 7, 45-48
    • (2002) Eur. Phys. J. e , vol.7 , pp. 45-48
    • Piazza, R.1    Iacopini, S.2
  • 48
    • 33751429390 scopus 로고
    • The Association Behavior of β-Lactoglobulins-A and β-Lactoglobulins-B
    • Timasheff, S. N.; Townend, R. The Association Behavior of β-Lactoglobulins-A and β-Lactoglobulins-B J. Am. Chem. Soc. 1958, 80, 4433-4434
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 4433-4434
    • Timasheff, S.N.1    Townend, R.2
  • 50
    • 33947468892 scopus 로고
    • Theory of Protein Titration Curves. 1. General Equations for Impenettrable Spheres
    • Tanford, C.; Kirkwood, J. G. Theory of Protein Titration Curves. 1. General Equations for Impenettrable Spheres J. Am. Chem. Soc. 1957, 79, 5333-5339
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 51
    • 0032658535 scopus 로고    scopus 로고
    • A Historical Introduction to Computer Models for Fractal Aggregates
    • Meakin, P. A Historical Introduction to Computer Models for Fractal Aggregates J. Sol-Gel Sci. Technol. 1999, 15, 97-117
    • (1999) J. Sol-Gel Sci. Technol. , vol.15 , pp. 97-117
    • Meakin, P.1
  • 52
    • 79955792632 scopus 로고    scopus 로고
    • Protein Purification by Polyelectrolyte Coacervation: Influence of Protein Charge Anisotropy on Selectivity
    • Xu, Y.; Mazzawi, M.; Chen, K.; Sun, L.; Dubin, P. L. Protein Purification by Polyelectrolyte Coacervation: Influence of Protein Charge Anisotropy on Selectivity Biomacromolecules 2011, 12, 1512-1522
    • (2011) Biomacromolecules , vol.12 , pp. 1512-1522
    • Xu, Y.1    Mazzawi, M.2    Chen, K.3    Sun, L.4    Dubin, P.L.5
  • 53
    • 33746260426 scopus 로고    scopus 로고
    • Monitoring and Modeling of Protein Processes Using Mass Spectrometry, Circular Dichroism, and Multivariate Curve Resolution Methods
    • Navea, S.; Tauler, R.; de Juan, A. Monitoring and Modeling of Protein Processes Using Mass Spectrometry, Circular Dichroism, and Multivariate Curve Resolution Methods Anal. Chem. 2006, 78, 4768-4778
    • (2006) Anal. Chem. , vol.78 , pp. 4768-4778
    • Navea, S.1    Tauler, R.2    De Juan, A.3
  • 55
    • 0033878843 scopus 로고    scopus 로고
    • Fractal Aggregation: Scaling of Fractal Dimension with Stability Ratio
    • Kim, A. Y.; Berg, J. C. Fractal Aggregation: Scaling of Fractal Dimension with Stability Ratio Langmuir 2000, 16, 2101-2104
    • (2000) Langmuir , vol.16 , pp. 2101-2104
    • Kim, A.Y.1    Berg, J.C.2
  • 56
    • 33947464992 scopus 로고
    • Hydrogen Ion Titration Curves of β-Lactoglobulin
    • Nozaki, Y.; Bunville, L. G.; Tanford, C. Hydrogen Ion Titration Curves of β-Lactoglobulin J. Am. Chem. Soc. 1959, 81, 5523-5529
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 5523-5529
    • Nozaki, Y.1    Bunville, L.G.2    Tanford, C.3
  • 57
    • 0037878962 scopus 로고
    • Double-Layer Forces between Heterogeneous Charged Surfaces
    • Miklavic, S. J.; Chan, D. Y. C.; White, L. R.; Healy, T. W. Double-Layer Forces between Heterogeneous Charged Surfaces J. Phys. Chem. 1994, 98, 9022-9032
    • (1994) J. Phys. Chem. , vol.98 , pp. 9022-9032
    • Miklavic, S.J.1    Chan, D.Y.C.2    White, L.R.3    Healy, T.W.4
  • 58
    • 84861864688 scopus 로고    scopus 로고
    • Effect of Charge Inhomogeneity and Mobility on Colloid Aggregation
    • Jho, Y. S.; Safran, S. A.; In, M.; Pincus, P. A. Effect of Charge Inhomogeneity and Mobility on Colloid Aggregation Langmuir 2012, 28, 8329-8336
    • (2012) Langmuir , vol.28 , pp. 8329-8336
    • Jho, Y.S.1    Safran, S.A.2    In, M.3    Pincus, P.A.4
  • 59
    • 32644465047 scopus 로고    scopus 로고
    • Long-Range Attraction between Charge-Mosaic Surfaces across Water
    • Perkin, S. K., N.; Klein, J. Long-Range Attraction between Charge-Mosaic Surfaces across Water Phys. Rev. Lett. 2006, 96, 038301
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 038301
    • Perkin, S.K.N.1    Klein, J.2


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