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Volumn 32, Issue 6, 2015, Pages 2072-2085

Purification and identification of High Molecular Weight Products formed during storage of neutral formulation of human insulin

Author keywords

High Molecular Weight Products (HMWP); Human insulin; Mass spectrometry; Reverse phase chromatography; Size exclusion chromatography

Indexed keywords

ACID ANHYDRIDE; HIGH MOLECULAR WEIGHT PRODUCT; HUMAN INSULIN; INSULIN; INSULIN DERIVATIVE; NEUTRAL INSULIN; UNCLASSIFIED DRUG; 4-CRESOL; AMINE; ANTIDIABETIC AGENT; CRESOL; INSULIN, NEUTRAL; PIG INSULIN; ZINC;

EID: 84934942708     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-014-1600-3     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm. 1999;185(2):129-88.
    • (1999) Int J Pharm , vol.185 , Issue.2 , pp. 129-188
    • Wang, W.1
  • 2
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE. Protein drug stability: a formulation challenge. Nat Rev Drug Discov. 2005;4(4):298-306.
    • (2005) Nat Rev Drug Discov , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 3
    • 3042761213 scopus 로고    scopus 로고
    • Structureimmunogenicity relationships of therapeutic proteins
    • Hermeling S, Crommelin DJ, Schellekens H, Jiskoot W. Structureimmunogenicity relationships of therapeutic proteins. Pharm Res. 2004;21(6):897-903.
    • (2004) Pharm Res , vol.21 , Issue.6 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.2    Schellekens, H.3    Jiskoot, W.4
  • 5
    • 33646546740 scopus 로고    scopus 로고
    • Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation
    • Hermeling S, Schellekens H, Maas C, Gebbink MF, Crommelin DJ, Jiskoot W. Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation. J Pharm Sci. 2006;95(5):1084-96.
    • (2006) J Pharm Sci , vol.95 , Issue.5 , pp. 1084-1096
    • Hermeling, S.1    Schellekens, H.2    Maas, C.3    Gebbink, M.F.4    Crommelin, D.J.5    Jiskoot, W.6
  • 6
    • 80054743161 scopus 로고    scopus 로고
    • Oxidized and aggregated recombinant human interferon beta is immunogenic in human interferon beta transgenic mice
    • van Beers MM, Sauerborn M, Gilli F, Brinks V, Schellekens H, Jiskoot W. Oxidized and aggregated recombinant human interferon beta is immunogenic in human interferon beta transgenic mice. Pharm Res. 2011;28(10):2393-402.
    • (2011) Pharm Res , vol.28 , Issue.10 , pp. 2393-2402
    • Van Beers, M.M.1    Sauerborn, M.2    Gilli, F.3    Brinks, V.4    Schellekens, H.5    Jiskoot, W.6
  • 7
    • 34250354402 scopus 로고    scopus 로고
    • Altered immunogenicity of isoaspartate containing proteins
    • Doyle HA, Gee RJ, Mamula MJ. Altered immunogenicity of isoaspartate containing proteins. Autoimmunity. 2007;40(2):131-7.
    • (2007) Autoimmunity , vol.40 , Issue.2 , pp. 131-137
    • Doyle, H.A.1    Gee, R.J.2    Mamula, M.J.3
  • 8
    • 0036001392 scopus 로고    scopus 로고
    • Insulin aspart (AspB28 human insulin) derivatives formed in pharmaceutical solutions
    • JarsMU, Hvass A, Waaben D. Insulin aspart (AspB28 human insulin) derivatives formed in pharmaceutical solutions. Pharm Res. 2002;19(5):621-8.
    • (2002) Pharm Res , vol.19 , Issue.5 , pp. 621-628
    • Jarsmu Hvass, A.1    Waaben, D.2
  • 9
    • 62749099087 scopus 로고    scopus 로고
    • Overlooking subvisible particles in therapeutic protein products: Gaps that may compromise product quality
    • Carpenter JF, Randolph TW, Jiskoot W, Crommelin DJ, Middaugh CR, Winter G, et al. Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality. J Pharm Sci. 2009;98(4):1201-5.
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1201-1205
    • Carpenter, J.F.1    Randolph, T.W.2    Jiskoot, W.3    Crommelin, D.J.4    Middaugh, C.R.5    Winter, G.6
  • 10
    • 84855872738 scopus 로고    scopus 로고
    • Protein instability and immunogenicity: Roadblocks to clinical application of injectable protein delivery systems for sustained release
    • Jiskoot W, Randolph TW, Volkin DB, Middaugh CR, Schöneich C, Winter G, et al. Protein instability and immunogenicity: roadblocks to clinical application of injectable protein delivery systems for sustained release. J Pharm Sci. 2012;101(3):946-54.
    • (2012) J Pharm Sci , vol.101 , Issue.3 , pp. 946-954
    • Jiskoot, W.1    Randolph, T.W.2    Volkin, D.B.3    Middaugh, C.R.4    Schöneich, C.5    Winter, G.6
  • 11
    • 77955100181 scopus 로고    scopus 로고
    • An industry perspective on the monitoring of subvisible particles as a quality attribute for protein therapeutics
    • Singh SK, Afonina N, Awwad M, Bechtold-Peters K, Blue JT, Chou D, et al. An industry perspective on the monitoring of subvisible particles as a quality attribute for protein therapeutics. J Pharm Sci. 2010;99(8):3302-21.
    • (2010) J Pharm Sci , vol.99 , Issue.8 , pp. 3302-3321
    • Singh, S.K.1    Afonina, N.2    Awwad, M.3    Bechtold-Peters, K.4    Blue, J.T.5    Chou, D.6
  • 12
    • 78650543555 scopus 로고    scopus 로고
    • Impact of product-related factors on immunogenicity of biotherapeutics
    • Singh SK. Impact of product-related factors on immunogenicity of biotherapeutics. J Pharm Sci. 2011;100(2):354-87.
    • (2011) J Pharm Sci , vol.100 , Issue.2 , pp. 354-387
    • Singh, S.K.1
  • 13
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006;8(3):501-7.
    • (2006) AAPS J , vol.8 , Issue.3 , pp. 501-507
    • Rosenberg, A.S.1
  • 15
    • 0027048535 scopus 로고
    • Chemical stability of insulin. 5. Isolation, characterization and identification of insulin transformation products
    • Brange J, Hallund O, Sørensen E. Chemical stability of insulin. 5. Isolation, characterization and identification of insulin transformation products. Acta Pharm Nord. 1992;4(4):223-32.
    • (1992) Acta Pharm Nord , vol.4 , Issue.4 , pp. 223-232
    • Brange, J.1    Hallund, O.2    Sørensen, E.3
  • 16
    • 0022517431 scopus 로고
    • The source of the circulating aggregate of insulin type i diabetic patients is therapeutic insulin
    • Maislos M, Mead PM, Gaynor DH, Robbins DC. The source of the circulating aggregate of insulin type I diabetic patients is therapeutic insulin. J Clin Invest. 1986;77(3):717-23.
    • (1986) J Clin Invest , vol.77 , Issue.3 , pp. 717-723
    • Maislos, M.1    Mead, P.M.2    Gaynor, D.H.3    Robbins, D.C.4
  • 17
    • 0027519426 scopus 로고
    • Immunogenicity and allergenic potential of animal and human insulins
    • Schernthaner G. Immunogenicity and allergenic potential of animal and human insulins. Diabetes Care. 1993;16(3):155-65.
    • (1993) Diabetes Care , vol.16 , Issue.3 , pp. 155-165
    • Schernthaner, G.1
  • 18
    • 0025286235 scopus 로고
    • Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates
    • Ratner ER, Phillips TM, Steiner M. Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates. Diabetes. 1990;39(6):728-33.
    • (1990) Diabetes , vol.39 , Issue.6 , pp. 728-733
    • Ratner, E.R.1    Phillips, T.M.2    Steiner, M.3
  • 19
    • 0023580282 scopus 로고
    • Free covalent aggregates of therapeutic insulin in blood of insulin-dependent diabetics
    • Robbins DC, Mead PM. Free covalent aggregates of therapeutic insulin in blood of insulin-dependent diabetics. Diabetes. 1987;36(2):147-51.
    • (1987) Diabetes , vol.36 , Issue.2 , pp. 147-151
    • Robbins, D.C.1    Mead, P.M.2
  • 21
    • 0028931574 scopus 로고
    • Evidence for a common intermediate in insulin deamidation and covalent dimer formation: Effects of pH and aniline trapping in dilute acidic solutions
    • Darrington RT, Anderson BD. Evidence for a common intermediate in insulin deamidation and covalent dimer formation: effects of pH and aniline trapping in dilute acidic solutions. J Pharm Sci. 1995;84(3):275-82.
    • (1995) J Pharm Sci , vol.84 , Issue.3 , pp. 275-282
    • Darrington, R.T.1    Anderson, B.D.2
  • 22
    • 0028998979 scopus 로고
    • Effects of insulin concentration and self-association on the partitioning of Its A-21 cyclic anhydride intermediate to desamido insulin and covalent dimer
    • Darrington RT, Anderson BD. Effects of insulin concentration and self-association on the partitioning of Its A-21 cyclic anhydride intermediate to desamido insulin and covalent dimer. Pharm Res. 1995;12(7):1077-84.
    • (1995) Pharm Res , vol.12 , Issue.7 , pp. 1077-1084
    • Darrington, R.T.1    Anderson, B.D.2
  • 23
    • 84866739512 scopus 로고    scopus 로고
    • Kinetics and mechanisms of deamidation and covalent amide-linked adduct formation in amorphous lyophiles of a model asparagine-containing peptide
    • DeHart MP, Anderson BD. Kinetics and mechanisms of deamidation and covalent amide-linked adduct formation in amorphous lyophiles of a model asparagine-containing peptide. Pharm Res. 2012;29(10):2722-37.
    • (2012) Pharm Res , vol.29 , Issue.10 , pp. 2722-2737
    • Dehart, M.P.1    Anderson, B.D.2
  • 24
    • 84864485477 scopus 로고    scopus 로고
    • Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: Covalent cross-linking via michael addition to tyrosine oxidation products
    • Torosantucci R, Mozziconacci O, Sharov V, Schöneich C, Jiskoot W. Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: covalent cross-linking via michael addition to tyrosine oxidation products. Pharm Res. 2012;29(8):2276-93.
    • (2012) Pharm Res , vol.29 , Issue.8 , pp. 2276-2293
    • Torosantucci, R.1    Mozziconacci, O.2    Sharov, V.3    Schöneich, C.4    Jiskoot, W.5
  • 25
    • 84455202363 scopus 로고    scopus 로고
    • Simultaneous detection and analysis of protein aggregation and protein unfolding by size exclusion chromatography with post column addition of fluorescent dye BisANS
    • Printz M, Friess W. Simultaneous detection and analysis of protein aggregation and protein unfolding by size exclusion chromatography with post column addition of fluorescent dye BisANS. J Pharm Sci. 2012;101(2):826-37.
    • (2012) J Pharm Sci , vol.101 , Issue.2 , pp. 826-837
    • Printz, M.1    Friess, W.2
  • 27
    • 0013913179 scopus 로고
    • Relationship of structure to biological activity of insulin as revealed by degradative studies
    • Carpenter FH. Relationship of structure to biological activity of insulin as revealed by degradative studies. Am J Med. 1966;40(5): 750-8.
    • (1966) Am J Med , vol.40 , Issue.5 , pp. 750-758
    • Carpenter, F.H.1
  • 28
    • 0026659078 scopus 로고
    • Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations
    • Brange J, Havelund S, Hougaard P. Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations. Pharm Res. 1992;9(6): 727-34.
    • (1992) Pharm Res , vol.9 , Issue.6 , pp. 727-734
    • Brange, J.1    Havelund, S.2    Hougaard, P.3
  • 31
    • 0028301459 scopus 로고
    • The role of intramolecular nucleophilic catalysis and the effects of self-association on the deamidation of human insulin at low pH
    • Darrington RT, Anderson BD. The role of intramolecular nucleophilic catalysis and the effects of self-association on the deamidation of human insulin at low pH. Pharm Res. 1994;11(6):784-93.
    • (1994) Pharm Res , vol.11 , Issue.6 , pp. 784-793
    • Darrington, R.T.1    Anderson, B.D.2
  • 32
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem. 1987;262(2):785-94.
    • (1987) J Biol Chem , vol.262 , Issue.2 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 33
    • 53849096676 scopus 로고    scopus 로고
    • Effect of ethylenediamine on chemical degradation of insulin aspart in pharmaceutical solutions
    • Poulsen C, Jacobsen D, Palm L. Effect of ethylenediamine on chemical degradation of insulin aspart in pharmaceutical solutions. Pharm Res. 2008;25(11):2534-44.
    • (2008) Pharm Res , vol.25 , Issue.11 , pp. 2534-2544
    • Poulsen, C.1    Jacobsen, D.2    Palm, L.3
  • 34
    • 0023918646 scopus 로고
    • Soluble, prolonged-acting insulin derivatives. III. Degree of protraction, crystallizability and chemical stability of insulins substituted in positions A21, B13, B23, B27 and B30
    • Markussen J, Diers I, Hougaard P, Langkjær L, Norris K, Snel L, et al. Soluble, prolonged-acting insulin derivatives. III. Degree of protraction, crystallizability and chemical stability of insulins substituted in positions A21, B13, B23, B27 and B30. Protein Eng. 1988;2(2):157-66.
    • (1988) Protein Eng , vol.2 , Issue.2 , pp. 157-166
    • Markussen, J.1    Diers, I.2    Hougaard, P.3    Langkjær, L.4    Norris, K.5    Snel, L.6
  • 35
    • 84905087622 scopus 로고    scopus 로고
    • Effects of phenol and meta-cresol depletion on insulin analog stability at physiological temperature
    • Teska BM, Alarcón J, Pettis RJ, Randolph TW, Carpenter JF. Effects of phenol and meta-cresol depletion on insulin analog stability at physiological temperature. J Pharm Sci. 2014;103(8):2255-67.
    • (2014) J Pharm Sci , vol.103 , Issue.8 , pp. 2255-2267
    • Teska, B.M.1    Alarcón, J.2    Pettis, R.J.3    Randolph, T.W.4    Carpenter, J.F.5
  • 36
    • 0026794132 scopus 로고
    • Chemical stability of insulin. 3. Influence of excipients, formulation, and pH
    • Brange J, Langkjær L. Chemical stability of insulin. 3. Influence of excipients, formulation, and pH. Acta Pharm Nord. 1992;4(4):149-58.
    • (1992) Acta Pharm Nord , vol.4 , Issue.4 , pp. 149-158
    • Brange, J.1    Langkjær, L.2
  • 38
    • 0024356816 scopus 로고
    • Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin and miniproinsulin
    • Kaarsholm NC, Ko HC, Dunn MF. Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin and miniproinsulin. Biochemistry. 1989;28(10):4427-35.
    • (1989) Biochemistry , vol.28 , Issue.10 , pp. 4427-4435
    • Kaarsholm, N.C.1    Ko, H.C.2    Dunn, M.F.3
  • 39
    • 33645972889 scopus 로고    scopus 로고
    • Asparagine deamidation: PH-dependent mechanism from density functional theory
    • Peters B, Trout BL. Asparagine deamidation: pH-dependent mechanism from density functional theory. Biochemistry. 2006;45(16): 5384-92.
    • (2006) Biochemistry , vol.45 , Issue.16 , pp. 5384-5392
    • Peters, B.1    Trout, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.