메뉴 건너뛰기




Volumn 28, Issue 8, 2010, Pages 863-869

Molecular dynamics simulation of the effect of ligand homogeneity on protein behavior in hydrophobic charge induction chromatography

Author keywords

Adsorption; Elution; Irreversibility; Molecular dynamics; Protein chromatography; Protein unfolding

Indexed keywords

ADSORPTION CHROMATOGRAPHY; AXIAL DIRECTION; COARSE GRAINED MODELS; COARSE-GRAINED; CONFORMATIONAL TRANSITIONS; ELECTROSTATIC REPULSION; EXPERIMENTAL TECHNIQUES; HETEROGENEOUS DISTRIBUTIONS; HYDROPHOBIC CHARGE INDUCTION CHROMATOGRAPHIES; HYDROPHOBIC INTERACTIONS; IN-LINE; LIGAND DENSITY; MATRIX; MICROSCOPIC BEHAVIOR; MOLECULAR DYNAMICS SIMULATIONS; PARAMETER OPTIMIZATION; PORE MODELS; POROUS ADSORBENT; PROTEIN ADSORPTION; PROTEIN BEHAVIOR; PROTEIN CHROMATOGRAPHY; PROTEIN CONFORMATION; PROTEIN ORIENTATION; PROTEIN UNFOLDING; RATIONAL DESIGN; STABLE ADSORPTION;

EID: 77951978883     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2010.03.006     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: a summary and pharmacological classification
    • Leader B., Baca Q.J., and Golan D.E. Protein therapeutics: a summary and pharmacological classification. Nat. Rev. Drug Discov. 7 (2008) 21-39
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 2
    • 1242341384 scopus 로고    scopus 로고
    • Expression systems for the production of recombinant pharmaceuticals
    • Sodoyer R. Expression systems for the production of recombinant pharmaceuticals. Biodrugs 18 (2004) 51-62
    • (2004) Biodrugs , vol.18 , pp. 51-62
    • Sodoyer, R.1
  • 3
    • 0031858337 scopus 로고    scopus 로고
    • Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers
    • Burton S.C., and Harding D.R. Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers. J. Chromatogr. A 814 (1998) 71-81
    • (1998) J. Chromatogr. A , vol.814 , pp. 71-81
    • Burton, S.C.1    Harding, D.R.2
  • 4
    • 0031555004 scopus 로고    scopus 로고
    • One step purification of chymosin by mixed mode chromatography
    • Burton S.C., Haggarty N.W., and Harding D.R. One step purification of chymosin by mixed mode chromatography. Biotechnol. Bioeng. 56 (1997) 45-55
    • (1997) Biotechnol. Bioeng. , vol.56 , pp. 45-55
    • Burton, S.C.1    Haggarty, N.W.2    Harding, D.R.3
  • 5
    • 0035951331 scopus 로고    scopus 로고
    • Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies
    • Schwartz W., Judd D., Wysocki M., Guerrier L., Birck-Wilson E., and Boschetti E. Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. J. Chromatogr. A 908 (2001) 251-263
    • (2001) J. Chromatogr. A , vol.908 , pp. 251-263
    • Schwartz, W.1    Judd, D.2    Wysocki, M.3    Guerrier, L.4    Birck-Wilson, E.5    Boschetti, E.6
  • 7
    • 0037023337 scopus 로고    scopus 로고
    • Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography
    • Weatherly G.T., Bouvier A., Lydiard D.D., Chapline J., Henderson I., Schrimsher J.L., and Shepard S.R. Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography. J. Chromatogr. A 952 (2002) 99-110
    • (2002) J. Chromatogr. A , vol.952 , pp. 99-110
    • Weatherly, G.T.1    Bouvier, A.2    Lydiard, D.D.3    Chapline, J.4    Henderson, I.5    Schrimsher, J.L.6    Shepard, S.R.7
  • 8
    • 0034468019 scopus 로고    scopus 로고
    • New method for the selective capture of antibodies under physiological conditions
    • Guerrier L., Girot P., Schwartz W., and Boschetti E. New method for the selective capture of antibodies under physiological conditions. Bioseparation 9 (2000) 211-221
    • (2000) Bioseparation , vol.9 , pp. 211-221
    • Guerrier, L.1    Girot, P.2    Schwartz, W.3    Boschetti, E.4
  • 9
    • 0035810718 scopus 로고    scopus 로고
    • A dual-mode approach to the selective separation of antibodies and their fragments
    • Guerrier L., Flayeux I., and Boschetti E. A dual-mode approach to the selective separation of antibodies and their fragments. J. Chromatogr. B 755 (2001) 37-46
    • (2001) J. Chromatogr. B , vol.755 , pp. 37-46
    • Guerrier, L.1    Flayeux, I.2    Boschetti, E.3
  • 10
    • 0036680280 scopus 로고    scopus 로고
    • Antibody separation by hydrophobic charge induction chromatography
    • Boschetti E. Antibody separation by hydrophobic charge induction chromatography. Trends Biotechnol. 20 (2002) 333-337
    • (2002) Trends Biotechnol. , vol.20 , pp. 333-337
    • Boschetti, E.1
  • 11
    • 34548185863 scopus 로고    scopus 로고
    • Displacement chromatography of proteins on hydrophobic charge induction adsorbent column
    • Zhao G.F., and Sun Y. Displacement chromatography of proteins on hydrophobic charge induction adsorbent column. J. Chromatogr. A 1165 (2007) 109-115
    • (2007) J. Chromatogr. A , vol.1165 , pp. 109-115
    • Zhao, G.F.1    Sun, Y.2
  • 12
    • 33745924699 scopus 로고    scopus 로고
    • Evaluation and comparison of alternatives to Protein A chromatography-mimetic and hydrophobic charge induction chromatographic stationary phases
    • Ghose S., Hubbard B., and Cramer S.M. Evaluation and comparison of alternatives to Protein A chromatography-mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A 1122 (2006) 144-152
    • (2006) J. Chromatogr. A , vol.1122 , pp. 144-152
    • Ghose, S.1    Hubbard, B.2    Cramer, S.M.3
  • 14
    • 54549111076 scopus 로고    scopus 로고
    • 5-Aminoindole, a new ligand for hydrophobic charge induction chromatography
    • Zhao G.F., Peng G.Y., Li F.Q., Shi Q.H., and Sun Y. 5-Aminoindole, a new ligand for hydrophobic charge induction chromatography. J. Chromatogr. A 1211 (2008) 90-98
    • (2008) J. Chromatogr. A , vol.1211 , pp. 90-98
    • Zhao, G.F.1    Peng, G.Y.2    Li, F.Q.3    Shi, Q.H.4    Sun, Y.5
  • 15
    • 38849101030 scopus 로고    scopus 로고
    • Patch controlled protein adsorption in mixed-mode chromatography with benzylamine as functional ligand
    • Gao D., Lin D.Q., and Yao S.J. Patch controlled protein adsorption in mixed-mode chromatography with benzylamine as functional ligand. Biochem. Eng. J. 38 (2008) 355-361
    • (2008) Biochem. Eng. J. , vol.38 , pp. 355-361
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3
  • 16
    • 35448950530 scopus 로고    scopus 로고
    • Mechanistic analysis on the effects of salt concentration and pH on protein adsorption onto a mixed-mode adsorbent with cation ligand
    • Gao D., Lin D.Q., and Yao S.J. Mechanistic analysis on the effects of salt concentration and pH on protein adsorption onto a mixed-mode adsorbent with cation ligand. J. Chromatogr. B 859 (2007) 16-23
    • (2007) J. Chromatogr. B , vol.859 , pp. 16-23
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3
  • 17
    • 33750451988 scopus 로고    scopus 로고
    • Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand
    • Gao D., Lin D.Q., and Yao S.J. Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand. Chem. Eng. Sci. 61 (2006) 7260-7268
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 7260-7268
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3
  • 18
    • 33746864462 scopus 로고    scopus 로고
    • Measurement and correlation of protein adsorption with mixed-mode adsorbents taking into account the influences of salt concentration and pH
    • Gao D., Lin D.Q., and Yao S.J. Measurement and correlation of protein adsorption with mixed-mode adsorbents taking into account the influences of salt concentration and pH. J. Chem. Eng. Data 51 (2006) 1205-1211
    • (2006) J. Chem. Eng. Data , vol.51 , pp. 1205-1211
    • Gao, D.1    Lin, D.Q.2    Yao, S.J.3
  • 19
    • 48449102579 scopus 로고    scopus 로고
    • Theoretical evaluation of methods for extracting retention factors and kinetic rate constants in liquid chromatography
    • Li X., and McGuffin V.L. Theoretical evaluation of methods for extracting retention factors and kinetic rate constants in liquid chromatography. J. Chromatogr. A 1203 (2008) 67-80
    • (2008) J. Chromatogr. A , vol.1203 , pp. 67-80
    • Li, X.1    McGuffin, V.L.2
  • 20
    • 67650096377 scopus 로고    scopus 로고
    • Molecular insight into protein conformational transition in hydrophobic charge induction chromatography: a molecular dynamics simulation
    • Zhang L., Zhao G.F., and Sun Y. Molecular insight into protein conformational transition in hydrophobic charge induction chromatography: a molecular dynamics simulation. J. Phys. Chem. B 113 (2009) 6873-6880
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6873-6880
    • Zhang, L.1    Zhao, G.F.2    Sun, Y.3
  • 21
    • 0025368288 scopus 로고
    • Metastability of the folded states of globular proteins
    • Honeycutt J.D., and Thirumalai D. Metastability of the folded states of globular proteins. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 3526-3529
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3526-3529
    • Honeycutt, J.D.1    Thirumalai, D.2
  • 22
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • Veitshans T., Klimov D., and Thirumalai D. Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties. Fold. Des. 2 (1997) 1-22
    • (1997) Fold. Des. , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.2    Thirumalai, D.3
  • 23
    • 36449009348 scopus 로고
    • Folding kinetics of proteins: a model study
    • Guo Z., and Thirumalai D. Folding kinetics of proteins: a model study. J. Chem. Phys. 97 (1992) 525-535
    • (1992) J. Chem. Phys. , vol.97 , pp. 525-535
    • Guo, Z.1    Thirumalai, D.2
  • 24
    • 0029010695 scopus 로고
    • Kinetics of protein folding: nucleation mechanism, time scales, and pathways
    • Guo Z., and Thirumalai D. Kinetics of protein folding: nucleation mechanism, time scales, and pathways. Biopolymers 36 (1995) 83-102
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 25
    • 12144266516 scopus 로고    scopus 로고
    • The competition between protein folding and aggregation: off-lattice minimalist model studies
    • Cellmer T., Bratko D., Prausnitz J.M., and Blanch H. The competition between protein folding and aggregation: off-lattice minimalist model studies. Biotechnol. Bioeng. 89 (2005) 78-87
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 78-87
    • Cellmer, T.1    Bratko, D.2    Prausnitz, J.M.3    Blanch, H.4
  • 26
    • 0346688724 scopus 로고    scopus 로고
    • Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models
    • Jang H.B., Hall C.K., and Zhou Y.Q. Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models. Biophys. J. 86 (2004) 31-49
    • (2004) Biophys. J. , vol.86 , pp. 31-49
    • Jang, H.B.1    Hall, C.K.2    Zhou, Y.Q.3
  • 27
    • 77649137571 scopus 로고    scopus 로고
    • Effects of ligand density on hydrophobic charge induction chromatography: molecular dynamics simulation
    • Zhang L., Zhao G.F., and Sun Y. Effects of ligand density on hydrophobic charge induction chromatography: molecular dynamics simulation. J. Phys. Chem. B 114 (2010) 2203-2211
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2203-2211
    • Zhang, L.1    Zhao, G.F.2    Sun, Y.3
  • 28
    • 0029633168 scopus 로고
    • Gromacs-a message-passing parallel molecular-dynamics implementation
    • Berendsen H.J., Vanderspoel D., and Vandrunen R. Gromacs-a message-passing parallel molecular-dynamics implementation. Comput. Phys. Commun. 91 (1995) 43-56
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.1    Vanderspoel, D.2    Vandrunen, R.3
  • 29
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van S.D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7 (2001) 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van, S.D.3
  • 30
    • 0029119568 scopus 로고
    • RASMOL-biomolecular graphics for all
    • Sayle R., and Milnerwhite E. RASMOL-biomolecular graphics for all. Trends Biochem. Sci. 20 (1995) 374-376
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 374-376
    • Sayle, R.1    Milnerwhite, E.2
  • 31
    • 60749123844 scopus 로고    scopus 로고
    • Dynamic control of protein conformation transition in chromatographic separation based on hydrophobic interactions: molecular dynamics simulation
    • Zhang L., Lu D.N., and Liu Z. Dynamic control of protein conformation transition in chromatographic separation based on hydrophobic interactions: molecular dynamics simulation. J. Chromatogr. A 1216 (2009) 2483-2490
    • (2009) J. Chromatogr. A , vol.1216 , pp. 2483-2490
    • Zhang, L.1    Lu, D.N.2    Liu, Z.3
  • 32
    • 41549155215 scopus 로고    scopus 로고
    • Oscillatory molecular driving force for protein folding at high concentration: a molecular simulation
    • Lu D.N., and Liu Z. Oscillatory molecular driving force for protein folding at high concentration: a molecular simulation. J. Phys. Chem. B 112 (2008) 2686-2693
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2686-2693
    • Lu, D.N.1    Liu, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.