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Volumn 102, Issue 3, 2013, Pages 947-959

Isomerization of Asp-Asp motif in model peptides and a monoclonal antibody fab fragment

Author keywords

Asp Asp motifs; Isomerization; Kinetics; Monoclonal antibody Fab

Indexed keywords

ASPARTIC ACID; HEXAPEPTIDE; IMMUNOGLOBULIN F(AB) FRAGMENT;

EID: 84878146568     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23423     Document Type: Article
Times cited : (22)

References (36)
  • 3
    • 0016859617 scopus 로고
    • Side reactions in peptide synthesis. II. Formation of succinimide derivatives from aspartyl residues
    • Bodanszky M, Natarajan S. 1975. Side reactions in peptide synthesis. II. Formation of succinimide derivatives from aspartyl residues. J Org Chem 40(17):2495-2499.
    • (1975) J Org Chem , vol.40 , Issue.17 , pp. 2495-2499
    • Bodanszky, M.1    Natarajan, S.2
  • 4
    • 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. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262(2):785-794.
    • (1987) J Biol Chem , vol.262 , Issue.2 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 7
    • 33846967443 scopus 로고    scopus 로고
    • Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies
    • Wakankar AA, Borchardt RT, Eigenbrot C, Shia S, Wang YJ, Shire SJ, Liu JL. 2007. Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies. Biochemistry 46(6):1534-1544.
    • (2007) Biochemistry , vol.46 , Issue.6 , pp. 1534-1544
    • Wakankar, A.A.1    Borchardt, R.T.2    Eigenbrot, C.3    Shia, S.4    Wang, Y.J.5    Shire, S.J.6    Liu, J.L.7
  • 9
    • 0030022071 scopus 로고    scopus 로고
    • Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity
    • Cacia J, Keck R, Presta LG, Frenz J. 1996. Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity. Biochemistry 35(6):1897-1903.
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 10
    • 0027463564 scopus 로고
    • Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide
    • Oliyai C, Borchardt RT. 1993. Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm Res 10(1):95-102.
    • (1993) Pharm Res , vol.10 , Issue.1 , pp. 95-102
    • Oliyai, C.1    Borchardt, R.T.2
  • 11
    • 0028260569 scopus 로고
    • Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides
    • Oliyai C, Borchardt RT. 1994. Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides. Pharm Res 11(5):751-758.
    • (1994) Pharm Res , vol.11 , Issue.5 , pp. 751-758
    • Oliyai, C.1    Borchardt, R.T.2
  • 13
    • 0024407404 scopus 로고
    • Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone
    • Johnson BA, Shirokawa JM, Hancock WS, Spellman MW, Basa LJ, Aswad DW. 1989. Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone. J Biol Chem 264(24):14262-14271.
    • (1989) J Biol Chem , vol.264 , Issue.24 , pp. 14262-14271
    • Johnson, B.A.1    Shirokawa, J.M.2    Hancock, W.S.3    Spellman, M.W.4    Basa, L.J.5    Aswad, D.W.6
  • 14
    • 0024379382 scopus 로고
    • Kinetics of the aspartyl transpeptidation of daptomycin, a novel lipopeptide antibiotic
    • Kirsch LE, Molloy RM, Debono M, Baker P, Farid KZ. 1989. Kinetics of the aspartyl transpeptidation of daptomycin, a novel lipopeptide antibiotic. Pharm Res 6(5):387-393.
    • (1989) Pharm Res , vol.6 , Issue.5 , pp. 387-393
    • Kirsch, L.E.1    Molloy, R.M.2    Debono, M.3    Baker, P.4    Farid, K.Z.5
  • 15
    • 0034829887 scopus 로고    scopus 로고
    • Neighboring side chain effects on asparaginyl and aspartyl degradation: An ab initio study of the relationship between peptide conformation and backbone NH acidity
    • Radkiewicz JL, Zipse H, Clarke S, Houk KN. 2001. Neighboring side chain effects on asparaginyl and aspartyl degradation: An ab initio study of the relationship between peptide conformation and backbone NH acidity. J Am Chem Soc 123(15):3499-3506.
    • (2001) J Am Chem Soc , vol.123 , Issue.15 , pp. 3499-3506
    • Radkiewicz, J.L.1    Zipse, H.2    Clarke, S.3    Houk, K.N.4
  • 16
    • 0024516367 scopus 로고
    • Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
    • Stephenson RC, Clarke S. 1989. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 264(11):6164-6170.
    • (1989) J Biol Chem , vol.264 , Issue.11 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 17
    • 0018122187 scopus 로고
    • Side reactions in peptide synthesis. VII. Sequence dependence in the formation of aminosuccinyl derivatives from beta-benzyl-aspartyl peptides
    • Bodanszky M, Kwei JZ. 1978. Side reactions in peptide synthesis. VII. Sequence dependence in the formation of aminosuccinyl derivatives from beta-benzyl-aspartyl peptides. Int J Pept Protein Res 12(2):69-74.
    • (1978) Int J Pept Protein Res , vol.12 , Issue.2 , pp. 69-74
    • Bodanszky, M.1    Kwei, J.Z.2
  • 18
    • 0029075220 scopus 로고
    • Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides
    • Brennan TV, Clarke S. 1995. Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides. Int J Pept Protein Res 45(6):547-553.
    • (1995) Int J Pept Protein Res , vol.45 , Issue.6 , pp. 547-553
    • Brennan, T.V.1    Clarke, S.2
  • 20
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar AA, Borchardt RT. 2006. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J Pharm Sci 95(11):2321-2336.
    • (2006) J Pharm Sci , vol.95 , Issue.11 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 21
    • 0027418664 scopus 로고
    • Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues-Effects of the solvent dielectric
    • Brennan TV, Clarke S. 1993. Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues-Effects of the solvent dielectric. Protein Sci 2(3):331-338.
    • (1993) Protein Sci , vol.2 , Issue.3 , pp. 331-338
    • Brennan, T.V.1    Clarke, S.2
  • 22
    • 41549106299 scopus 로고    scopus 로고
    • Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody
    • Xiao G, Bondarenko PV. 2008. Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody. J Pharm Biomed Anal 47(1):23-30.
    • (2008) J Pharm Biomed Anal , vol.47 , Issue.1 , pp. 23-30
    • Xiao, G.1    Bondarenko, P.V.2
  • 23
    • 79551550805 scopus 로고    scopus 로고
    • Identification of isomerization and racemization of aspartate in the Asp-Asp motifs of a therapeutic protein
    • Zhang J, Yip H, Katta V. 2011. Identification of isomerization and racemization of aspartate in the Asp-Asp motifs of a therapeutic protein. Anal Biochem 410(2):234-243.
    • (2011) Anal Biochem , vol.410 , Issue.2 , pp. 234-243
    • Zhang, J.1    Yip, H.2    Katta, V.3
  • 24
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis KJ, Morrison JF. 1982. Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol 87:405-426.
    • (1982) Methods Enzymol , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 26
    • 79956148004 scopus 로고    scopus 로고
    • Specific racemization of heavy-chain cysteine-220 in the hinge region of immunoglobulin gamma 1 as a possible cause of degradation during storage
    • Amano M, Hasegawa J, Kobayashi N, Kishi N, Nakazawa T, Uchiyama S, Fukui K. Specific racemization of heavy-chain cysteine-220 in the hinge region of immunoglobulin gamma 1 as a possible cause of degradation during storage. Anal Chem 83(10):3857-3864.
    • Anal Chem , vol.83 , Issue.10 , pp. 3857-3864
    • Amano, M.1    Hasegawa, J.2    Kobayashi, N.3    Kishi, N.4    Nakazawa, T.5    Uchiyama, S.6    Fukui, K.7
  • 27
    • 77957372613 scopus 로고    scopus 로고
    • Kinetics of aspartic acid isomerization and enantiomerization in model aspartyl tripeptides under forced conditions
    • Conrad U, Fahr A, Scriba GKE. 2010. Kinetics of aspartic acid isomerization and enantiomerization in model aspartyl tripeptides under forced conditions. J Pharm Sci 99(10):4162-4173.
    • (2010) J Pharm Sci , vol.99 , Issue.10 , pp. 4162-4173
    • Conrad, U.1    Fahr, A.S.G.2
  • 28
    • 0242489004 scopus 로고    scopus 로고
    • Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry
    • De Boni S, Oberthur C, Hamburger M, Scriba GK. 2004. Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry. J Chromatogr A 1022(1-2):95-102.
    • (2004) J Chromatogr A , vol.1022 , Issue.1-2 , pp. 95-102
    • De, B.S.1    Oberthur, C.2    Hamburger, M.3    Scriba, G.K.4
  • 29
    • 82555168019 scopus 로고    scopus 로고
    • Determination of rate constants for β-linkage isomerization of three specific aspartyl residues in recombinant human αA-crystallin protein by reversed-phase HPLC
    • Sadakane Y, Fujii N, Nakagomi K. 2011. Determination of rate constants for β-linkage isomerization of three specific aspartyl residues in recombinant human αA-crystallin protein by reversed-phase HPLC. J Chromatogr B, Anal Technol Biomed Life Sci 879(29):3240-3246.
    • (2011) J Chromatogr B, Anal Technol Biomed Life Sci , vol.879 , Issue.29 , pp. 3240-3246
    • Sadakane, Y.1    Fujii, N.2    Nakagomi, K.3
  • 30
    • 37049082534 scopus 로고
    • Kinetics and mechanism of the reversible isomerization of aspartic acid residues in tetrapeptides
    • Capasso S, Kirby AJ, Salvadori S, Sica F, Zagari A. 1995. Kinetics and mechanism of the reversible isomerization of aspartic acid residues in tetrapeptides. J Chem Soc, Perkin Trans 2(3):437-442.
    • (1995) J Chem Soc, Perkin Trans , vol.2 , Issue.3 , pp. 437-442
    • Capasso, S.1    Kirby, A.J.2    Salvadori, S.3    Sica, F.4    Zagari, A.5
  • 31
    • 0026185519 scopus 로고
    • Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts, buffers and organic solvents
    • Capasso S, Mazzarella L, Zagari A. 1991. Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts, buffers and organic solvents. Peptide Res 4(4):234-238.
    • (1991) Peptide Res , vol.4 , Issue.4 , pp. 234-238
    • Capasso, S.1    Mazzarella, L.2    Zagari, A.3
  • 32
    • 0025024815 scopus 로고
    • Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide
    • Patel K, Borchardt RT. 1990. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm Res 7(7):703-711.
    • (1990) Pharm Res , vol.7 , Issue.7 , pp. 703-711
    • Patel, K.1    Borchardt, R.T.2
  • 33
    • 16444383511 scopus 로고    scopus 로고
    • Effects of acidic N + 1 residues on asparagine deamidation rates in solution and in the solid state
    • Li B, Gorman EM, Moore KD, Williams T, Schowen RL, Topp EM, Borchardt RT. 2005. Effects of acidic N + 1 residues on asparagine deamidation rates in solution and in the solid state. J Pharm Sci 94(3):666-675.
    • (2005) J Pharm Sci , vol.94 , Issue.3 , pp. 666-675
    • Li, B.1    Gorman, E.M.2    Moore, K.D.3    Williams, T.4    Schowen, R.L.5    Topp, E.M.6    Borchardt, R.T.7
  • 34
    • 79961009713 scopus 로고    scopus 로고
    • Accurate determination of succinimide degradation products using high fidelity trypsin digestion peptide map analysis
    • Yu XC, Joe K, Zhang Y, Adriano A, Wang Y, Gazzano-Santoro H, Keck RG, Deperalta G, Ling V. 2011. Accurate determination of succinimide degradation products using high fidelity trypsin digestion peptide map analysis. Anal Chem 83(15):5912-5919.
    • (2011) Anal Chem , vol.83 , Issue.15 , pp. 5912-5919
    • Yu, X.C.1    Joe, K.2    Zhang, Y.3    Adriano, A.4    Wang, Y.5    Gazzano-Santoro, H.6    Keck, R.G.7    Deperalta, G.8    Ling, V.9
  • 35
    • 67749109890 scopus 로고    scopus 로고
    • Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody
    • Sinha S, Zhang L, Duan S, Williams TD, Vlasak J, Ionescu R, Topp EM. 2009. Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody. Protein Sci 18(8):1573-1584.
    • (2009) Protein Sci , vol.18 , Issue.8 , pp. 1573-1584
    • Sinha, S.1    Zhang, L.2    Duan, S.3    Williams, T.D.4    Vlasak, J.5    Ionescu, R.6    Topp, E.M.7
  • 36
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • Xie M, Schowen RL. 1999. Secondary structure and protein deamidation. J Pharm Sci 88(1):8-13.
    • (1999) J Pharm Sci , vol.88 , Issue.1 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2


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