Qualification of a Quantitative Method for Monitoring Aspartate Isomerization of a Monoclonal Antibody by Focused Peptide Mapping

Reference

1. 1.↵
   1. Geiger T.,
   2. 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), 785–794.

   OpenUrlAbstract/FREE Full Text
2. 2.↵
   1. Manning M. C.,
   2. Patel K.,
   3. Borchardt R. T.

   Stability of Protein Pharmaceuticals. Pharm. Res. 1989, 6 (11), 903–918.

   OpenUrlCrossRefPubMedWeb of Science
3. 3.↵
   1. Cacia J.,
   2. Keck R.,
   3. Presta L. G.,
   4. Frenz J.

   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 1996, 35 (6), 1897–1903.

   OpenUrlCrossRefPubMedWeb of Science
4. 4.↵
   1. Wakankar A. A.,
   2. Borchardt R. T.,
   3. Eigenbrot C.,
   4. Shia S.,
   5. Wang Y. J.,
   6. Shire S. J.,
   7. Liu J. L.

   Aspartate Isomerization in the Complementarity-determining Regions of Two Closely Related Monoclonal Antibodies. Biochemistry 2007, 46 (6), 1534–1544.

   OpenUrlCrossRefPubMedWeb of Science
5. 5.↵
   1. Cloos P. A.,
   2. Fledelius C.

   Collagen Fragments in Urine Derived from Bone Resorption Are Highly Racemized and Isomerized: a Biological Clock of Protein Aging with Clinical Potential. Biochem. J. 2000, 345 (3), 473–480.

   OpenUrlAbstract/FREE Full Text
6. 6.↵
   1. Clarke S.

   Propensity for Spontaneous Succinimide Formation from Aspartyl and Asparaginyl Residues in Cellular Proteins. Int. J. Pept. Protein Res. 1987, 30 (6), 808–821.

   OpenUrlPubMedWeb of Science
7. 7.↵
   1. Oliyai C.,
   2. Borchardt R. T.

   Chemical Pathways of Peptide Degradation. VI. Effect of the Primary Sequence on the Pathways of Degradation of Aspartyl Residues in Model Hexapeptides. Pharm. Res. 1994, 11 (5), 751–758.

   OpenUrlCrossRefPubMedWeb of Science
8. 8.↵
   1. Chu G. C.,
   2. Chelius D.,
   3. Xiao G.,
   4. Khor H. K.,
   5. Coulibaly S.,
   6. Bondarenko P. V.

   Accumulation of Succinimide in a Recombinant Monoclonal Antibody in Mildly Acidic Buffers under Elevated Temperatures. Pharm. Res. 2007, 24 (6), 1145–1156.

   OpenUrlPubMed
9. 9.↵
   1. Xiao G.,
   2. Bondarenko P. V.

   Identification and Quantification of Degradations in the Asp-Asp Motifs of a Recombinant Monoclonal Antibody. J. Pharm. Biomed. Anal. 2008, 47 (1), 23–30.

   OpenUrlPubMed
10. 10.↵
    1. Zhang J.,
    2. Yip H.,
    3. Katta V.

    Identification of Isomerization and Racemization of Aspartate in the Asp-Asp Motifs of a Therapeutic Protein. Anal. Biochem. 2011, 410 (2), 234–243.

    OpenUrlPubMed
11. 11.↵
    1. Yi L.,
    2. Beckley N.,
    3. Gikanga B.,
    4. Zhang J.,
    5. Wang Y. J.,
    6. Chih H. W.,
    7. Sharma V. K.

    Isomerization of Asp-Asp Motif in Model Peptides and a Monoclonal Antibody Fab Fragment. J. Pharm. Sci. 2013, 102 (3), 947–959.

    OpenUrlCrossRefPubMed
12. 12.↵
    1. Mire-Sluis A. R

    State of the Art Analytical Methods for the Characterization of Biological Products and Assessment of Comparability, Mire-Sluis A. R, Ed.; Karger: Basel, Switzerland, 2005; pp 117–127.
13. 13.↵
    1. Rehder D. S.,
    2. Chelius D.,
    3. McAuley A.,
    4. Dillon T. M.,
    5. Xiao G.,
    6. Crouse-Zeineddini J.,
    7. Vardanyan L.,
    8. Perico N.,
    9. Mukku V.,
    10. Brems D. N.,
    11. Matsumura M.,
    12. Bondarenko P. V.

    Isomerization of a Single Aspartyl Residue of Anti-epidermal Growth Factor Receptor Immunoglobulin Gamma2 Antibody Highlights the Role Avidity Plays in Antibody Activity. Biochemistry 2008, 47 (8), 2518–2530.

    OpenUrl
14. 14.↵
    1. Doyle H. A.,
    2. Gee R. J.,
    3. Mamula M. J.

    Altered Immunogenicity of Isoaspartate Containing Proteins. Autoimmunity 2007, 40 (2), 131–137.

    OpenUrlCrossRefPubMedWeb of Science
15. 15.↵
    1. Cournoyer J. J.,
    2. Pittman J. L.,
    3. Ivleva V. B.,
    4. Fallows E.,
    5. Waskell L.,
    6. Costello C. E.,
    7. o'Conner P. B.

    Deamidation: Differentiation of Aspartyl from Isoaspartyl Products in Peptides by Electron Capture Dissociation. Protein Sci. 2005, 14 (2), 452–463.

    OpenUrlCrossRefPubMed
16. 16.↵
    1. O'Connor P. B.,
    2. Cournoyer J. J.,
    3. Pitteri S. J.,
    4. Chrisman P. A.,
    5. McLuckey S. A.

    Differentiation of Aspartic and Isoaspartic Acids Using Electron Transfer Dissociation. J. Am. Soc. Mass. Spectr. 2006, 17 (1),15–19.

    OpenUrlCrossRefPubMedWeb of Science
17. 17.↵
    1. Johnson B. A.,
    2. Aswad D. W.

    Optimal Conditions for the Use of Protein L–Isoaspartyl Methyltransferase in Assessing the Isoaspartate Content of Peptides and Proteins. Anal. Biochem. 1991, 192 (2), 384–391.

    OpenUrlCrossRefPubMed
18. 18.↵
    1. Carlson A. D.,
    2. Riggin R. M.

    Development of Improved High-performance Liquid Chromatography Conditions for Nonisotopic Detection of Isoaspartic Acid To Determine the Extent of Protein Deamidation. Anal. Biochem. 2000, 278 (2), 150–155.

    OpenUrlCrossRefPubMed
19. 19.↵
    1. Zhang W.,
    2. Czupryn J. M.,
    3. Boyle P. T. Jr..,
    4. Amari J.

    Characterization of Asparagine Deamidation and Aspartate Isomerization in Recombinant Human Interleukin-11. Pharm. Res. 2002, 19 (8), 1223–1231.

    OpenUrlPubMed
20. 20.↵
    1. Zhang W.,
    2. Czupryn M. J.

    Development of a Strong Cation-exchange High-performance Liquid Chromatography Method for Analysis of Isoaspartate in Proteins. Anal. Biochem. 2002, 307 (1), 184–186.

    OpenUrlPubMed
21. 21.↵
    1. Diepold K.,
    2. Bomans K.,
    3. Wiedmann M.,
    4. Zimmermann B.,
    5. Petzold A.,
    6. Schlothauer T.,
    7. Mueller R.,
    8. Moritz B.,
    9. Stracke J. O.,
    10. Mølhøj M.,
    11. Reusch D.,
    12. Bulau P.

    Simultaneous Assessment of Asp Isomerization and Asn Deamidation in Recombinant Antibodies by LC-MS Following Incubation at Elevated Temperatures. PLoS One 2012, 7 (1), e30295.

    OpenUrlPubMed
22. 22.↵
    1. Eakin C. M.,
    2. Miller A.,
    3. Kerr J.,
    4. Kung J.,
    5. Wallace A.

    Assessing Analytical Methods To Monitor IsoAsp Formation in Monoclonal Antibodies. Front. Pharmacol. 2014, 5, 87.

    OpenUrl
23. 23.↵
    Guidance for Industry. Q7A. Good Manufacturing Practice Guidance for Active Pharmaceutical Ingredients. Available from http://www.fda.gov/Drugs/GuidanceComplianceRegulatoryInformation/Guidances/ucm065005.htm.
24. 24.↵
    1. Wyndham K. D.,
    2. O'Gara J. E.,
    3. Walter T. H.,
    4. Glose K. H.,
    5. Lawrence N. L.,
    6. Alden B. A.,
    7. Izzo G. S.,
    8. Hudalla C. J.,
    9. Iraneta P. C.

    Characterization and Evaluation of C18 HPLC Stationary Phases Based on Ethyl-bridged Hybrid Organic/Inorganic Particles. Anal. Chem. 2003, 75 (24), 6781–6788.

    OpenUrlCrossRefPubMed
25. 25.↵
    1. Peng L.,
    2. Oganesyan V.,
    3. Wu H.,
    4. Dall'Acqua W. F.,
    5. Damschroder M. M.

    Molecular Basis for Antagonistic Activity of Anifrolumab, an Anti-interferon–Alpha Receptor 1 Antibody. MAbs 2015, 7 (2), 428–439.

    OpenUrlCrossRefPubMed