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Volumn 101, Issue 10, 2012, Pages 3651-3660

Relating particle formation to salt- and pH-dependent phase separation of non-native aggregates of alpha-chymotrypsinogen A

Author keywords

Biotechnology; Microparticles; Physical stability; Protein aggregation; Protein formulation; Solubility

Indexed keywords

ANION; CHYMOTRYPSINOGEN; MONOMER; SODIUM CHLORATE; SODIUM CHLORIDE; THIOCYANATE;

EID: 84865369923     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23264     Document Type: Article
Times cited : (17)

References (38)
  • 3
    • 80053039882 scopus 로고    scopus 로고
    • Experimental detection and characterization of protein aggregates
    • John Wiley & Sons, Inc.
    • Sharma VK, Kalonia DS. 2010. Experimental detection and characterization of protein aggregates. In Aggregation of therapeutic proteins. John Wiley & Sons, Inc., pp 205-256.
    • (2010) Aggregation of therapeutic proteins , pp. 205-256
    • Sharma, V.K.1    Kalonia, D.S.2
  • 4
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded.
    • Uversky VN, Fink AL. 2004. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta 1698(2):131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , Issue.2 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 5
    • 84862945390 scopus 로고    scopus 로고
    • Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc
    • Latypov RF, Hogan S, Lau H, Gadgil H, Liu D. 2011. Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc. J Biol Chem 287(2):1381-1396.
    • (2011) J Biol Chem , vol.287 , Issue.2 , pp. 1381-1396
    • Latypov, R.F.1    Hogan, S.2    Lau, H.3    Gadgil, H.4    Liu, D.5
  • 6
    • 78049270959 scopus 로고    scopus 로고
    • Acid-induced aggregation of human monoclonal IgG1 and IgG2: Molecular mechanism and the effect of solution composition
    • Hari SB, Lau H, Razinkov VI, Chen S, Latypov RF. 2010. Acid-induced aggregation of human monoclonal IgG1 and IgG2: Molecular mechanism and the effect of solution composition. Biochemistry 49(43):9328-9338.
    • (2010) Biochemistry , vol.49 , Issue.43 , pp. 9328-9338
    • Hari, S.B.1    Lau, H.2    Razinkov, V.I.3    Chen, S.4    Latypov, R.F.5
  • 7
    • 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 RK, Nesta DP, Chang L, Chase SF, Laue TM, Roberts CJ. 2011. Nonnative aggregation of an IgG1 antibody in acidic conditions, Part 1: Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J Pharm Sci 100(6):2087-2103.
    • (2011) J Pharm Sci , vol.100 , Issue.6 , 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
  • 8
    • 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 RK, Nesta DP, Chang L, Kroetsch AM, Roberts CJ. 2011. Nonnative aggregation of an IgG1 antibody in acidic conditions, Part 2: Nucleation and growth kinetics with competing growth mechanisms. J Pharm Sci 100(6):2104-2119.
    • (2011) J Pharm Sci , vol.100 , Issue.6 , pp. 2104-2119
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Kroetsch, A.M.4    Roberts, C.J.5
  • 9
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth
    • Weiss WF, Hodgdon TK, Kaler EW, Lenhoff AM, Roberts CJ. 2007. Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth. Biophys J 93(12):4392-4403.
    • (2007) Biophys J , vol.93 , Issue.12 , pp. 4392-4403
    • Weiss, W.F.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 11
    • 80054767747 scopus 로고    scopus 로고
    • Protein aggregation and particle formation: Effects of formulation, interfaces, and drug product manufacturing operations
    • John Wiley & Sons, Inc.
    • Mahler H, Fischer S, Randolph TW, Carpenter JF. 2010. Protein aggregation and particle formation: Effects of formulation, interfaces, and drug product manufacturing operations. In Aggregation of therapeutic proteins. John Wiley & Sons, Inc., pp 301-331.
    • (2010) Aggregation of therapeutic proteins , pp. 301-331
    • Mahler, H.1    Fischer, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 12
    • 74049123780 scopus 로고    scopus 로고
    • Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A
    • Li Y, Ogunnaike BA, Roberts CJ. 2010. Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A. J Pharm Sci 99(2):645-662.
    • (2010) J Pharm Sci , vol.99 , Issue.2 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 13
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews JM, Roberts CJ. 2007. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111(27):7897-7913.
    • (2007) J Phys Chem B , vol.111 , Issue.27 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 14
    • 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 CJ. 2009. Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization. J Phys Chem B 113(19):7020-7032.
    • (2009) J Phys Chem B , vol.113 , Issue.19 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 15
    • 79952092133 scopus 로고    scopus 로고
    • Computational design and biophysical characterization of aggregation-resistant point mutations for γD crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity
    • Sahin E, Jordan JL, Spatara ML, Naranjo A, Costanzo JA, Weiss WF, Robinson AS, Fernandez EJ, Roberts CJ. 2011. Computational design and biophysical characterization of aggregation-resistant point mutations for γD crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity. Biochemistry 50(5):628-639.
    • (2011) Biochemistry , vol.50 , Issue.5 , pp. 628-639
    • Sahin, E.1    Jordan, J.L.2    Spatara, M.L.3    Naranjo, A.4    Costanzo, J.A.5    Weiss, W.F.6    Robinson, A.S.7    Fernandez, E.J.8    Roberts, C.J.9
  • 16
    • 77949812737 scopus 로고    scopus 로고
    • Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics
    • Rao G, Iyer V, Kosloski MP, Pisal DS, Shin E, Middaugh CR, Balu-Iyer SV. 2010. Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics. J Pharm Sci 99(4):1697-1706.
    • (2010) J Pharm Sci , vol.99 , Issue.4 , pp. 1697-1706
    • Rao, G.1    Iyer, V.2    Kosloski, M.P.3    Pisal, D.S.4    Shin, E.5    Middaugh, C.R.6    Balu-Iyer, S.V.7
  • 17
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies
    • Sahin E, Grillo AO, Perkins MD, Roberts CJ. 2010. Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. J Pharm Sci 99(12):4830-4848.
    • (2010) J Pharm Sci , vol.99 , Issue.12 , pp. 4830-4848
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 18
  • 19
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris AM, Watzky MA, Finke RG. 2009. Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. Biochim Biophys Acta 1794(3):375-397.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.3 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 20
    • 84875617666 scopus 로고    scopus 로고
    • Size-exclusion chromatography with multi-angle light scattering (SEC-MALS) for elucidating protein aggregation mechanisms
    • 2nd ed. Springer, Humana Press. In press
    • Sahin E, Roberts CJ. Size-exclusion chromatography with multi-angle light scattering (SEC-MALS) for elucidating protein aggregation mechanisms. In Therapeutic proteins: Methods and protocols. 2nd ed. Springer, Humana Press. In press.
    • Therapeutic proteins: Methods and protocols
    • Sahin, E.1    Roberts, C.J.2
  • 22
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life
    • Roberts CJ. 2003. Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life. J Phys Chem B 107(5):1194-1207.
    • (2003) J Phys Chem B , vol.107 , Issue.5 , pp. 1194-1207
    • Roberts, C.J.1
  • 23
    • 70349646469 scopus 로고    scopus 로고
    • Characterization of high-molecular-weight non-native aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering
    • Li Y, Weiss WF, Roberts CJ. 2009. Characterization of high-molecular-weight non-native aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering. J Pharm Sci 98(11):3997-4016.
    • (2009) J Pharm Sci , vol.98 , Issue.11 , pp. 3997-4016
    • Li, Y.1    Weiss, W.F.2    Roberts, C.J.3
  • 24
    • 34250870678 scopus 로고    scopus 로고
    • Non-native aggregation of α-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies
    • Andrews JM, Roberts CJ. 2007. Non-native aggregation of α-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies. Biochemistry 46(25):7558-7571.
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7558-7571
    • Andrews, J.M.1    Roberts, C.J.2
  • 25
    • 39749110693 scopus 로고    scopus 로고
    • Nucleation, growth, and activation energies for seeded and unseeded aggregation of α-chymotrypsinogen A
    • Andrews JM, Weiss WF, Roberts CJ. 2008. Nucleation, growth, and activation energies for seeded and unseeded aggregation of α-chymotrypsinogen A. Biochemistry 47(8):2397-2403.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2397-2403
    • Andrews, J.M.1    Weiss, W.F.2    Roberts, C.J.3
  • 26
    • 78650154417 scopus 로고    scopus 로고
    • Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology
    • Zhang A, Jordan JL, Ivanova MI, Weiss WF, Roberts CJ, Fernandez EJ. 2010. Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology. Biochemistry 49(49):10553-10564.
    • (2010) Biochemistry , vol.49 , Issue.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
  • 27
    • 77956102828 scopus 로고    scopus 로고
    • Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH
    • Ako K, Nicolai T, Durand D, Brotons G. 2009. Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH. Soft Matter 5(20):4033.
    • (2009) Soft Matter , vol.5 , Issue.20 , pp. 4033
    • Ako, K.1    Nicolai, T.2    Durand, D.3    Brotons, G.4
  • 28
    • 0000953383 scopus 로고    scopus 로고
    • Using phase transitions to investigate the effect of salts on protein interactions
    • Broide ML, Tominc TM, Saxowsky MD. 1996. Using phase transitions to investigate the effect of salts on protein interactions. Phys Rev E 53(6):6325-6335.
    • (1996) Phys Rev E , vol.53 , Issue.6 , pp. 6325-6335
    • Broide, M.L.1    Tominc, T.M.2    Saxowsky, M.D.3
  • 29
    • 0034611647 scopus 로고    scopus 로고
    • Mechanisms of phase behaviour and protein partitioning in detergent/polymer aqueous two-phase systems for purification of integral membrane proteins
    • Sivars U, Tjerneld F. 2000. Mechanisms of phase behaviour and protein partitioning in detergent/polymer aqueous two-phase systems for purification of integral membrane proteins. Biochim Biophys Acta 1474(2):133-146.
    • (2000) Biochim Biophys Acta , vol.1474 , Issue.2 , pp. 133-146
    • Sivars, U.1    Tjerneld, F.2
  • 31
    • 0001202494 scopus 로고
    • Amino-acid sequence of bovine chymotrypsinogen-A
    • Hartley BS. 1964. Amino-acid sequence of bovine chymotrypsinogen-A. Nature 201(4926):1284-1287.
    • (1964) Nature , vol.201 , Issue.4926 , pp. 1284-1287
    • Hartley, B.S.1
  • 33
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. 1996. How Hofmeister ion interactions affect protein stability. Biophys J 71(4):2056-2063.
    • (1996) Biophys J , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 34
    • 84875616869 scopus 로고    scopus 로고
    • Effects of dimer seeding and Hofmeister salts on the mechanism and kinetics of nonnative micro-particle formation for alpha-chymotrypsinogen A. In preparation.
    • Brummitt RK, Pagels RK, Morris AM, Remmele RLJ, Roberts CJ. Effects of dimer seeding and Hofmeister salts on the mechanism and kinetics of nonnative micro-particle formation for alpha-chymotrypsinogen A. In preparation.
    • Brummitt, R.K.1    Pagels, R.K.2    Morris, A.M.3    Remmele, R.L.J.4    Roberts, C.J.5
  • 36
    • 0037104813 scopus 로고    scopus 로고
    • The influence of ionic dispersion potentials on counterion condensation on polyelectrolytes
    • Boström M, Williams DRM, Ninham BW. 2012. The influence of ionic dispersion potentials on counterion condensation on polyelectrolytes. J Phys Chem B 106(32):7908-7912.
    • (2012) J Phys Chem B , vol.106 , Issue.32 , pp. 7908-7912
    • Boström, M.1    Williams, D.R.M.2    Ninham, B.W.3
  • 37
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98(5):927-938.
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1


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