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Volumn 100, Issue 4, 2011, Pages 1306-1315

Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: Role of conformational and colloidal stability

Author keywords

Calorimetry (DSC); Colloidal stability; Conformational stability; Fluorescence spectroscopy; Formulation; High throughput screening stability; Light scattering; Monoclonal antibody; Protein aggregation

Indexed keywords

FLUORESCENT DYE; MONOCLONAL ANTIBODY; PROTEIN AGGREGATE;

EID: 79951895571     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22371     Document Type: Article
Times cited : (137)

References (32)
  • 2
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185(2):129-188.
    • (1999) Int J Pharm , vol.185 , Issue.2 , pp. 129-188
    • Wang, W.1
  • 3
    • 0032940238 scopus 로고    scopus 로고
    • Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
    • Welfle K, Misselwitz R, Hausdorf G, Höhne W, Welfle H. 1999. Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments. Biochim Biophys Acta 1431(1):120-131.
    • (1999) Biochim Biophys Acta , vol.1431 , Issue.1 , pp. 120-131
    • Welfle, K.1    Misselwitz, R.2    Hausdorf, G.3    Höhne, W.4    Welfle, H.5
  • 5
    • 0141535431 scopus 로고    scopus 로고
    • Preformulation studies as an essential guide to formulation development and manufacture of protein pharmaceuticals
    • Volkin DB, Sanyal G, Burke CJ, Middaugh CR. 2002. Preformulation studies as an essential guide to formulation development and manufacture of protein pharmaceuticals. Pharm Biotechnol 14:1-46.
    • (2002) Pharm Biotechnol , vol.14 , pp. 1-46
    • Volkin, D.B.1    Sanyal, G.2    Burke, C.J.3    Middaugh, C.R.4
  • 6
    • 33845923234 scopus 로고    scopus 로고
    • High throughput screening of protein formulation stability: Practical considerations
    • Capelle MAH, Gurny R, Arvinte T. 2007. High throughput screening of protein formulation stability: Practical considerations. Eur J Pharm Biopharm 65(2):131-148.
    • (2007) Eur J Pharm Biopharm , vol.65 , Issue.2 , pp. 131-148
    • Capelle, M.A.H.1    Gurny, R.2    Arvinte, T.3
  • 7
    • 27644469867 scopus 로고    scopus 로고
    • Solution behavior of IFN-beta-1a: An empirical phase diagram based approach
    • Fan H, Ralston J, Dibiase M, Faulkner E, Middaugh CR. 2005. Solution behavior of IFN-beta-1a: An empirical phase diagram based approach. J Pharm Sci 94(9):1893-1911.
    • (2005) J Pharm Sci , vol.94 , Issue.9 , pp. 1893-1911
    • Fan, H.1    Ralston, J.2    Dibiase, M.3    Faulkner, E.4    Middaugh, C.R.5
  • 9
    • 4444301974 scopus 로고    scopus 로고
    • Rational design of solution additives for the prevention of protein aggregation
    • Baynes BM, Trout BL. 2004. Rational design of solution additives for the prevention of protein aggregation. Biophys J 87(3):1631-1639.
    • (2004) Biophys J , vol.87 , Issue.3 , pp. 1631-1639
    • Baynes, B.M.1    Trout, B.L.2
  • 10
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 11
    • 0031708329 scopus 로고    scopus 로고
    • Recent advances in our understanding of protein conformational stability from a pharmaceutical perspective
    • Middaugh CR, Edwards KL. 1998. Recent advances in our understanding of protein conformational stability from a pharmaceutical perspective. Expert Opin Investig Drugs 7(9):1493-1500.
    • (1998) Expert Opin Investig Drugs , vol.7 , Issue.9 , pp. 1493-1500
    • Middaugh, C.R.1    Edwards, K.L.2
  • 13
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289(1-2):1-30.
    • (2005) Int J Pharm , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 14
    • 0033922354 scopus 로고    scopus 로고
    • Thermal unfolding and refolding of beta-lactoglobulin. An intrinsic andextrinsic fluorescence study
    • Bhattacharjee C, Das KP. 2000. Thermal unfolding and refolding of beta-lactoglobulin. An intrinsic andextrinsic fluorescence study. Eur J Biochem 267(13):3957-3964.
    • (2000) Eur J Biochem , vol.267 , Issue.13 , pp. 3957-3964
    • Bhattacharjee, C.1    Das, K.P.2
  • 15
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A, Sutter M, Jiskoot W. 2008. Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25(7):1487-1499.
    • (2008) Pharm Res , vol.25 , Issue.7 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 16
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor
    • Cummings MD, Farnum MA, Nelen MI. 2006. Universal screening methods and applications of ThermoFluor. J Biomol Screen 11(7):854-863.
    • (2006) J Biomol Screen , vol.11 , Issue.7 , pp. 854-863
    • Cummings, M.D.1    Farnum, M.A.2    Nelen, M.I.3
  • 19
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P. 2006. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357(2):289-298.
    • (2006) Anal Biochem , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 20
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F, Hogan S, Latypov RF, Narhi LO, Razinkov VI. 2009. High throughput thermostability screening of monoclonal antibody formulations. J Pharm Sci 9(4):1707-1720.
    • (2009) J Pharm Sci , vol.9 , Issue.4 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 21
    • 0036525843 scopus 로고    scopus 로고
    • Kinetics of protein aggregation. Quantitative estimation of the chaperone-like activity in test-systems based on suppression of protein aggregation
    • Kurganov BI. 2002. Kinetics of protein aggregation. Quantitative estimation of the chaperone-like activity in test-systems based on suppression of protein aggregation. Biochemistry (Mosc) 67(4):409-422.
    • (2002) Biochemistry (Mosc) , vol.67 , Issue.4 , pp. 409-422
    • Kurganov, B.I.1
  • 22
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra GA, Markin E, Yamazaki K, Hui R, Vedadi M, Awrey DE. 2006. Screening for ligands using a generic and high-throughput light-scattering-based assay. J Biomol Screen 11(8):940-948.
    • (2006) J Biomol Screen , vol.11 , Issue.8 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5    Awrey, D.E.6
  • 23
    • 71549161144 scopus 로고    scopus 로고
    • Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability
    • Fast JL, Cordes AA, Carpenter JF, Randolph TW. 2009. Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability. Biochemistry 48(49):11724-11736.
    • (2009) Biochemistry , vol.48 , Issue.49 , pp. 11724-11736
    • Fast, J.L.1    Cordes, A.A.2    Carpenter, J.F.3    Randolph, T.W.4
  • 24
    • 36749040335 scopus 로고    scopus 로고
    • Nonnative protein aggregation kinetics
    • Roberts CJ. 2007. Nonnative protein aggregation kinetics. Biotechnol Bioeng 98(5):927-938.
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 25
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WFt, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98(4):1246-1277.
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1246-1277
    • Weiss, W.F.1    Young, T.M.2    Roberts, C.J.3
  • 27
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R, Eyring H. 1954. Conformation changes of proteins. J Phys Chem 58(2):110-120.
    • (1954) J Phys Chem , vol.58 , Issue.2 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 28
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff SN. 2002. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 41(46):13473-13482.
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13473-13482
    • Timasheff, S.N.1
  • 29
    • 0029198906 scopus 로고
    • Solvent stabilization of protein structure
    • Timasheff SN. 1995. Solvent stabilization of protein structure. Methods Mol Biol 40:253-269.
    • (1995) Methods Mol Biol , vol.40 , pp. 253-269
    • Timasheff, S.N.1
  • 30
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose
    • Kaushik JK, Bhat R. 2003. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J Biol Chem 278(29):26458-26465.
    • (2003) J Biol Chem , vol.278 , Issue.29 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 31
    • 34548290876 scopus 로고    scopus 로고
    • Mechanism of solvent induced thermal stabilization of papain
    • Sathish HA, Kumar PR, Prakash V. 2007. Mechanism of solvent induced thermal stabilization of papain. Int J Biol Macromol 41(4):383-390.
    • (2007) Int J Biol Macromol , vol.41 , Issue.4 , pp. 383-390
    • Sathish, H.A.1    Kumar, P.R.2    Prakash, V.3
  • 32
    • 67349269275 scopus 로고    scopus 로고
    • Role of electrostatic repulsion on colloidal stability of Bacillus halmapalus alpha-amylase
    • Olsen SN, Andersen KB, Randolph TW, Carpenter JF, Westh P. 2009. Role of electrostatic repulsion on colloidal stability of Bacillus halmapalus alpha-amylase. Biochim Biophys Acta 1794(7):1058-1065.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.7 , pp. 1058-1065
    • Olsen, S.N.1    Andersen, K.B.2    Randolph, T.W.3    Carpenter, J.F.4    Westh, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.