메뉴 건너뛰기




Volumn 453, Issue 2, 2013, Pages 351-357

Evaluating the inter and intra batch variability of protein aggregation behaviour using Taylor dispersion analysis and dynamic light scattering

Author keywords

Aggregation; Biosimilar; Dynamic light scattering; Hydrodynamic radius; Taylor dispersion analysis

Indexed keywords

A 2058; A 2153; A 8654; BOVINE SERUM ALBUMIN; EXCIPIENT; UNCLASSIFIED DRUG;

EID: 84884147610     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2013.05.062     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 84884126395 scopus 로고    scopus 로고
    • CFR320, Title 21 U.S. Food and Drug Administration (FDA)
    • CFR320, 2004. Code of Federal Regulations. Title 21, Volume 5. U.S. Food and Drug Administration (FDA).
    • (2004) Code of Federal Regulations , vol.5
  • 2
    • 42949106938 scopus 로고    scopus 로고
    • Study of thermally and chemically unfolded conformations of bovine serum albumin by means of dynamic light scattering
    • Aschi, A., Mbarek, N., Othman, M., Gharbi, A., 2008. Study of thermally and chemically unfolded conformations of bovine serum albumin by means of dynamic light scattering. Mater. Sci. Eng. C 28, 594-600.
    • (2008) Mater. Sci. Eng. C , vol.28 , pp. 594-600
    • Aschi, A.1    Mbarek, N.2    Othman, M.3    Gharbi, A.4
  • 3
    • 79953681018 scopus 로고    scopus 로고
    • Immunogenicity of biotherapeutics in the context of developing biosimilars and biobetters
    • Barbosa, D.F.S., 2011. Immunogenicity of biotherapeutics in the context of developing biosimilars and biobetters. Drug Discov. Today 16 (7/8), 345-353.
    • (2011) Drug Discov. Today , vol.16 , Issue.7-8 , pp. 345-353
    • Barbosa, D.F.S.1
  • 4
    • 23444457779 scopus 로고    scopus 로고
    • Characterization of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic condition
    • DOI 10.1016/j.bbapap.2005.06.007, PII S1570963905001779
    • Brahma, A., Mandal, C., Bhattacharyya, D., 2005a. Characterisation of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic condition. Biochim. Biophys. Acta 1751, 159-169. (Pubitemid 41112234)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1751 , Issue.2 , pp. 159-169
    • Brahma, A.1    Mandal, C.2    Bhattacharyya, D.3
  • 5
    • 71749108118 scopus 로고    scopus 로고
    • Nonclinical development of biopharmaceuticals
    • Baumann, A., 2009. Nonclinical development of biopharmaceuticals. Drug Discov. Today 14, 1112-1122.
    • (2009) Drug Discov. Today , vol.14 , pp. 1112-1122
    • Baumann, A.1
  • 6
    • 23444457779 scopus 로고    scopus 로고
    • Characterization of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic condition
    • DOI 10.1016/j.bbapap.2005.06.007, PII S1570963905001779
    • Brahma, A., Mandal, C., Bhattacharyya, D., 2005b. Characterisation of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic conditions. Biochim. Biophys. Acta 1751, 159-169. (Pubitemid 41112234)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1751 , Issue.2 , pp. 159-169
    • Brahma, A.1    Mandal, C.2    Bhattacharyya, D.3
  • 8
    • 21444442363 scopus 로고    scopus 로고
    • Biosimilar epoetins: An analysis based on recently implemented European Medicines Evaluation Agency guidelines on comparability of biopharmaceutical proteins
    • DOI 10.1592/phco.2005.25.7.954
    • Combe, C., Tredree, R.L., Schellekens, H., 2005. Biosimilar epo etins: an analysis based on recently implemented European medicines evaluation agency guidelines on comparability of biopharmaceutical proteins. Pharmacotherapy 25 (7), 954-962. (Pubitemid 40917928)
    • (2005) Pharmacotherapy , vol.25 , Issue.7 , pp. 954-962
    • Combe, C.1    Tredree, R.L.2    Schellekens, H.3
  • 9
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell, M.E., Hilario, E., Jacobson, F., 2006. Protein aggregation and bioprocessing. AAPS J. 8 (3), 572-579.
    • (2006) AAPS J. , vol.8 , Issue.3 , pp. 572-579
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 11
    • 80054742841 scopus 로고    scopus 로고
    • Taylor dispersion analysis compared to dynamic light scattering for the size analysis of therapeutic peptides and proteins and their aggregates
    • Hawe, A., Hulse, W.L., Jiskoot, W., Forbes, R.T., 2011. Taylor dispersion analysis compared to dynamic light scattering for the size analysis of therapeutic peptides and proteins and their aggregates. Pharm. Res. 28 (9), 2302-2310.
    • (2011) Pharm. Res. , vol.28 , Issue.9 , pp. 2302-2310
    • Hawe, A.1    Hulse, W.L.2    Jiskoot, W.3    Forbes, R.T.4
  • 12
    • 79955967866 scopus 로고    scopus 로고
    • A nanolitre method to determine the hydrodynamic radius of proteins and small molecules by Taylor dispersion analysis
    • Hulse, W.L., Forbes, R.T., 2011a. A nanolitre method to determine the hydrodynamic radius of proteins and small molecules by Taylor dispersion analysis. Int. J. Pharm. 411, 64-68.
    • (2011) Int. J. Pharm. , vol.411 , pp. 64-68
    • Hulse, W.L.1    Forbes, R.T.2
  • 13
    • 80051790195 scopus 로고    scopus 로고
    • A Taylor dispersion analysis method for the sizing of therapeutic proteins and their aggregates using nanolitre sample quantities
    • Hulse, W.L., Forbes, R.T., 2011b. A Taylor dispersion analysis method for the sizing of therapeutic proteins and their aggregates using nanolitre sample quantities. Int. J. Pharm. 416, 394-397.
    • (2011) Int. J. Pharm. , vol.416 , pp. 394-397
    • Hulse, W.L.1    Forbes, R.T.2
  • 14
    • 84860764287 scopus 로고    scopus 로고
    • A comparison of the pharmacodynamic behavior of branded and biosimilar enoxaparin in primates
    • Jeske, W., Litinas, E., Khan, H., Happensteaddt, D., Fareed, J., 2012. A comparison of the pharmacodynamic behavior of branded and biosimilar enoxaparin in primates. Clin. Appl. Thromb Hemost. 18 (3), 294-298.
    • (2012) Clin. Appl. Thromb Hemost. , vol.18 , Issue.3 , pp. 294-298
    • Jeske, W.1    Litinas, E.2    Khan, H.3    Happensteaddt, D.4    Fareed, J.5
  • 15
    • 0020520881 scopus 로고
    • Variability in different lots of commercial bovine serum albumin affects cell multiplication and hatching of rabbit blastocysts in culture
    • Kane, M.T., 1983. Variability in different lots of commercial bovine serum albumin affects cell multiplication and hatching of rabbit blastocysts in culture. J. Reprod. Fert. 69, 555-558. (Pubitemid 13021959)
    • (1983) Journal of Reproduction and Fertility , vol.69 , Issue.2 , pp. 555-558
    • Kane, M.T.1
  • 17
    • 67449138587 scopus 로고    scopus 로고
    • Biosimilars-science, status and strategic perspective
    • Kresse, G.-B., 2009. Biosimilars-science, status and strategic perspective. Eur. J. Pharm. Biopharm. 72, 479-486.
    • (2009) Eur. J. Pharm. Biopharm. , vol.72 , pp. 479-486
    • Kresse, G.-B.1
  • 18
  • 19
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry, R., Eyring, H., 1953. Conformation changes of proteins. J. Phys. Chem. 58, 110-120.
    • (1953) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 20
    • 0035922871 scopus 로고    scopus 로고
    • Mechanism of bovine serum albumin aggregation during ultrafiltration
    • DOI 10.1002/bit.10001
    • Maruyama, T., Katoh, S., Nakajima, M., Nabetani, H., 2001. Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotech. Bioeng. 75 (2), 233-238. (Pubitemid 32937295)
    • (2001) Biotechnology and Bioengineering , vol.75 , Issue.2 , pp. 233-238
    • Maruyama, T.1    Katoh, S.2    Nakajima, M.3    Nabetani, H.4
  • 21
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • DOI 10.1016/j.bpc.2003.09.004
    • Militello, V., Casarno, C., Emanuele, A., Giostra, A., Pullara, F., Pullara, F., Leone, M., 2004. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 107, 175-187. (Pubitemid 38220958)
    • (2004) Biophysical Chemistry , vol.107 , Issue.2 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 23
    • 0020435643 scopus 로고
    • Nonspecific stabilisation of stress-susceptible proteins by stress resistant proteins; a model for the biological role of heat shock proteins
    • Minton, K.W., Karmin, G.M., Hahn Minton, A.P., 1982. Nonspecific stabilisation of stress-susceptible proteins by stress resistant proteins; a model for the biological role of heat shock proteins. Biochemistry 79, 7107-7111.
    • (1982) Biochemistry , vol.79 , pp. 7107-7111
    • Minton, K.W.1    Karmin, G.M.2    Hahn Minton, A.P.3
  • 24
    • 0042526640 scopus 로고    scopus 로고
    • The immunogenicity of biopharmaceuticals. Lessons learned and consequences for protein drug development
    • Basel
    • Patten, P.A., Schellekens, H., 2003. The immunogenicity of biopharmaceuticals. Lessons learned and consequences for protein drug development. Dev. Biol. (Basel) 112, 81-97.
    • (2003) Dev. Biol. , vol.112 , pp. 81-97
    • Patten, P.A.1    Schellekens, H.2
  • 25
    • 1042287178 scopus 로고    scopus 로고
    • Regulatory considerations of pharmaceutical solid polymorphism in Abbreviated New Drug Applications (ANDAs)
    • Raw, A.S., Furness, M.S., Gill, D.S., Adams, R.C., Holcombe Jr., F.O., Yu, L.X., 2004. Regulatory considerations of pharmaceutical solid polymorphism in Abbreviated New Drug Applications (ANDAs). Adv. Drug Deliv. Rev. 56, 391-414.
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 391-414
    • Raw, A.S.1    Furness, M.S.2    Gill, D.S.3    Adams, R.C.4    Holcombe Jr., F.O.5    Yu, L.X.6
  • 27
    • 67349221747 scopus 로고    scopus 로고
    • Assesing the bioequivalence of biosimilars
    • Schellekens, H., 2009. Assesing the bioequivalence of biosimilars. Drug Discov. Today 14 (9/10), 495-499.
    • (2009) Drug Discov. Today , vol.14 , Issue.9-10 , pp. 495-499
    • Schellekens, H.1
  • 29
    • 75349094554 scopus 로고    scopus 로고
    • Characterisation of different conformations of bovine serum albumin and their propensity to aggregate in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide
    • Sharma, A., Agarwal, P.K., Deep, S., 2010. Characterisation of different conformations of bovine serum albumin and their propensity to aggregate in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide. J. Coll. Int. Sci. 343, 454-462.
    • (2010) J. Coll. Int. Sci. , vol.343 , pp. 454-462
    • Sharma, A.1    Agarwal, P.K.2    Deep, S.3
  • 32
    • 77249086523 scopus 로고    scopus 로고
    • Biosimilars approval process
    • Zuniga, L., Calvo, B., 2010. Biosimilars approval process. Regul. Toxicol. Pharmacol. 56 (3), 374-377.
    • (2010) Regul. Toxicol. Pharmacol. , vol.56 , Issue.3 , pp. 374-377
    • Zuniga, L.1    Calvo, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.