Citation: | Katharina Böttinger, Christof Regl, Veronika Schäpertöns, Erdmann Rapp, Therese Wohlschlager, Christian G. Huber. “Small is beautiful”-examining reliable determination of low-abundant therapeutic antibody glycovariants[J]. Journal of Pharmaceutical Analysis. doi: 10.1016/j.jpha.2024.100982 |
[1] |
C. Reily, T.J. Stewart, M.B. Renfrow, J. Novak, Glycosylation in health and disease, Nat. Rev. Nephrol. 2019156. 15(2019) 346-366. https://doi.org/10.1038/s41581-019- 0129-4.
|
[2] |
M. Schiestl, T. Stangler, C. Torella, T. Čepeljnik, H. Toll, R. Grau, Acceptable changes in quality attributes of glycosylated biopharmaceuticals, Nat. Biotechnol. 29(2011) 310- 312. https://doi.org/10.1038/nbt.1839.
|
[3] |
T. Wohlschlager, K. Scheffler, I.C. Forstenlehner, W. Skala, S. Senn, E. Damoc, J. Holzmann, C.G. Huber, Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals, Nat. Commun. 9(2018) 1-9. https://doi.org/10.1038/s41467-018-04061-7.
|
[4] |
A. Beck, H. Liu, Macro- and Micro-Heterogeneity of Natural and Recombinant IgG Antibodies, Antibodies. 8(2019) 18. https://doi.org/10.3390/antib8010018.
|
[5] |
M. Thomann, K. Reckermann, D. Reusch, J. Prasser, M.L. Tejada, Fc-galactosylation modulates antibody-dependent cellular cytotoxicity of therapeutic antibodies, Mol. Immunol. 73(2016) 69-75. https://doi.org/10.1016/j.molimm.2016.03.002.
|
[6] |
Y. Kaneko, F. Nimmerjahn, J. V. Ravetch, Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation, Science (80-.). 313(2006) 670-673. https://doi.org/10.1126/SCIENCE.1129594/SUPPL_FILE/KANEKO.SOM.PDF.
|
[7] |
V.S. Shivatare, P.K. Chuang, T.H. Tseng, Y.F. Zeng, H.W. Huang, G. Veeranjaneyulu, H.C. Wu, C.H. Wong, Study on antibody Fc-glycosylation for optimal effector functions, Chem. Commun. (2023). https://doi.org/10.1039/d3cc00672g.
|
[8] |
S.A. Berkowitz, J.R. Engen, J.R. Mazzeo, G.B. Jones, Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars, Nat. Rev. Drug Discov. 11(2012) 527-540. https://doi.org/10.1038/nrd3746.
|
[9] |
ICH HARMONISED TRIPARTITE GUIDELINE:Specifications:Test Procedures and Acceptance Criteria for Biotechnological/Biological Products-Q6B, (n.d.). https://database.ich.org/sites/default/files/Q6B Guideline.pdf.
|
[10] |
S. Carillo, R. Pérez-Robles, C. Jakes, M. Ribeiro da Silva, S. Millán Martín, A. Farrell, N. Navas, J. Bones, Comparing different domains of analysis for the characterisation of N-glycans on monoclonal antibodies, J. Pharm. Anal. 10(2020) 23-34. https://doi.org/10.1016/j.jpha.2019.11.008.
|
[11] |
N. De Haan, M. Pučić-Baković, M. Novokmet, D. Falck, G. Lageveen-Kammeijer, G. Razdorov, F. Vučković, I. Trbojević-Akmačić, O. Gornik, M. Hanić, M. Wuhrer, G. Lauc, A. Guttman, R. Cummings, S. Mora, Y. Rombouts, A. Mehta, Developments and perspectives in high-throughput protein glycomics:enabling the analysis of thousands of samples, Glycobiology. 32(2022) 651-663. https://doi.org/10.1093/glycob/cwac026.
|
[12] |
X. Liu, Z. Sun, Z. Li, Y. Zhang, H. Lu, Mass spectrometry-based analysis of IgG glycosylation and its applications, Int. J. Mass Spectrom. 474(2022) 116799. https://doi.org/10.1016/j.ijms.2022.116799.
|
[13] |
W. Skala, T. Wohlschlager, S. Senn, G.E. Huber, C.G. Huber, MoFi:A Software Tool for Annotating Glycoprotein Mass Spectra by Integrating Hybrid Data from the Intact Protein and Glycopeptide Level, Anal. Chem. 90(2018) 5728-5736. https://doi.org/10.1021/acs.analchem.8b00019.
|
[14] |
S. Millán-Martín, C. Jakes, S. Carillo, T. Buchanan, M. Guender, D.B. Kristensen, T.M. Sloth, M. Ørgaard, K. Cook, J. Bones, Inter-laboratory study of an optimised peptide mapping workflow using automated trypsin digestion for monitoring monoclonal antibody product quality attributes, Anal. Bioanal. Chem. (2020) 1-16. https://doi.org/10.1007/s00216-020-02809-z.
|
[15] |
C.I. Butré, V. D'Atri, H. Diemer, O. Colas, E. Wagner, A. Beck, S. Cianferani, D. Guillarme, A. Delobel, Interlaboratory Evaluation of a User-Friendly Benchtop Mass Spectrometer for Multiple-Attribute Monitoring Studies of a Monoclonal Antibody, Mol. 2023, Vol. 28, Page 2855. 28(2023) 2855. https://doi.org/10.3390/MOLECULES28062855.
|
[16] |
M.L.A. De Leoz, D.L. Duewer, A. Fung, L. Liu, H.K. Yau, O. Potter, G.O. Staples, K. Furuki, R. Frenkel, Y. Hu, Z. Sosic, P. Zhang, F. Altmann, C. Grunwald-Grube, C. Shao, J. Zaia, W. Evers, S. Pengelley, D. Suckau, A. Wiechmann, A. Resemann, W. Jabs, A. Beck, J.W. Froehlich, C. Huang, Y. Li, Y. Liu, S. Sun, Y. Wang, Y. Seo, H.J. An, N.C. Reichardt, J.E. Ruiz, S. Archer-Hartmann, P. Azadi, L. Bell, Z. Lakos, Y. An, J.F. Cipollo, M. Pucic-Bakovic, J. Štambuk, G. Lauc, X. Li, P.G. Wang, A. Bock, R. Hennig, E. Rapp, M. Creskey, T.D. Cyr, M. Nakano, T. Sugiyama, P.K.A. Leung, P. LinkLenczowski, J. Jaworek, S. Yang, H. Zhang, T. Kelly, S. Klapoetke, R. Cao, J.Y. Kim, H.K. Lee, J.Y. Lee, J.S. Yoo, S.R. Kim, S.K. Suh, N. De Haan, D. Falck, G.S.M. Lageveen-Kammeijer, M. Wuhrer, R.J. Emery, R.P. Kozak, L.P. Liew, L. Royle, P.A. Urbanowicz, N.H. Packer, X. Song, A. Everest-Dass, E. Lattová, S. Cajic, K. Alagesan, D. Kolarich, T. Kasali, V. Lindo, Y. Chen, K. Goswami, B. Gau, R. Amunugama, R. Jones, C.J.M. Stroop, K. Kato, H. Yagi, S. Kondo, C.T. Yuen, A. Harazono, X. Shi, P.E. Magnelli, B.T. Kasper, L. Mahal, D.J. Harvey, R. O'Flaherty, P.M. Rudd, R. Saldova, E.S. Hecht, D.C. Muddiman, J. Kang, P. Bhoskar, D. Menard, A. Saati, C. Merle, S. Mast, S. Tep, J. Truong, T. Nishikaze, S. Sekiya, A. Shafer, S. Funaoka, M. Toyoda, P. De Vreugd, C. Caron, P. Pradhan, N.C. Tan, Y. Mechref, S. Patil, J.S. Rohrer, R. Chakrabarti, D. Dadke, M. Lahori, C. Zou, C. Cairo, B. Reiz, R.M. Whittal, C.B. Lebrilla, L. Wu, A. Guttman, M. Szigeti, B.G. Kremkow, K.H. Lee, C. Sihlbom, B. Adamczyk, C. Jin, N.G. Karlsson, J. Örnros, G. Larson, J. Nilsson, B. Meyer, A. Wiegandt, E. Komatsu, H. Perreault, E.D. Bodnar, N. Said, Y.N. Francois, E. LeizeWagner, S. Maier, A. Zeck, A.J.R. Heck, Y. Yang, R. Haselberg, Y.Q. Yu, W. Alley, J.W. Leone, H. Yuan, S.E. Stein, NIST interlaboratory study on glycosylation analysis of monoclonal antibodies:Comparison of results from diverse analytical methods, Mol. Cell. Proteomics. 19(2020) 11-30. https://doi.org/10.1074/mcp.RA119.001677.
|
[17] |
M. Bern, T. Caval, Y.J. Kil, W. Tang, C. Becker, E. Carlson, D. Kletter, K.I. Sen, N. Galy, D. Hagemans, V. Franc, A.J.R. Heck, Parsimonious Charge Deconvolution for Native Mass Spectrometry, J. Proteome Res. 17(2018) 1216-1226. https://doi.org/10.1021/acs.jproteome.7b00839.
|
[18] |
S. Millán-Martín, S. Carillo, F. Füssl, J. Sutton, P. Gazis, K. Cook, K. Scheffler, J. Bones, Optimisation of the use of sliding window deconvolution for comprehensive characterisation of trastuzumab and adalimumab charge variants by native high resolution mass spectrometry, Eur. J. Pharm. Biopharm. 158(2021) 83-95. https://doi.org/10.1016/j.ejpb.2020.11.006.
|
[19] |
K. Böttinger, W. Esser-Skala, M. Segl, C. Herwig, C.G. Huber, At-line quantitative profiling of monoclonal antibody products during bioprocessing using HPLC-MS, Anal. Chim. Acta. 1207(2022) 339813. https://doi.org/10.1016/J.ACA.2022.339813.
|
[20] |
F. Di Marco, T. Berger, W. Esser-skala, E. Rapp, C. Regl, C.G. Huber, Simultaneous monitoring of monoclonal antibody variants by strong cation-exchange chromatography hyphenated to mass spectrometry to assess quality attributes of rituximab-based biotherapeutics, Int. J. Mol. Sci. 22(2021). https://doi.org/10.3390/ijms22169072.
|
[21] |
B. MacLean, D.M. Tomazela, N. Shulman, M. Chambers, G.L. Finney, B. Frewen, R. Kern, D.L. Tabb, D.C. Liebler, M.J. MacCoss, Skyline:an open source document editor for creating and analyzing targeted proteomics experiments, Bioinformatics. 26(2010) 966-968. https://doi.org/10.1093/BIOINFORMATICS/BTQ054.
|
[22] |
W. Esser-Skala, T. Wohlschlager, C. Regl, C.G. Huber, A Simple Strategy to Eliminate Hexosylation Bias in the Relative Quantification of N-glycosylation in Biopharmaceuticals, Angew. Chemie Int. Ed. (2020) anie.202002147. https://doi.org/10.1002/anie.202002147.
|
[23] |
M. Lebede, F. Di Marco, W. Esser-Skala, R. Hennig, T. Wohlschlager, C.G. Huber, Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes:An Expedition along Different Structural Levels of Human Chorionic Gonadotropin by Employing Mass Spectrometry, Anal. Chem. 93(2021) 10424-10434. https://doi.org/10.1021/ACS.ANALCHEM.1C02199/SUPPL_FILE/AC1C02199_SI_003.ZIP.
|
[24] |
R. Hennig, S. Cajic, M. Borowiak, M. Hoffmann, R. Kottler, U. Reichl, E. Rapp, Towards personalized diagnostics via longitudinal study of the human plasma Nglycome, Biochim. Biophys. Acta-Gen. Subj. 1860(2016) 1728-1738. https://doi.org/10.1016/J.BBAGEN.2016.03.035.
|
[25] |
C.H. Gao, G. Yu, P. Cai, ggVennDiagram:An Intuitive, Easy-to-Use, and Highly Customizable R Package to Generate Venn Diagram, Front. Genet. 12(2021) 1598. https://doi.org/10.3389/FGENE.2021.706907/BIBTEX.
|
[26] |
N. Hulstaert, J. Shofstahl, T. Sachsenberg, M. Walzer, H. Barsnes, L. Martens, Y. PerezRiverol, ThermoRawFileParser:Modular, Scalable, and Cross-Platform RAW File Conversion, J. Proteome Res. 19(2020) 537-542. https://doi.org/10.1021/acs.jproteome.9b00328.
|
[27] |
H. Wickham, W. Chang, L. Henry, T.L. Pedersen, K. Takahashi, C. Wilke, K. Woo, H. Yutani, D. Dunnington, ggplot2:Create Elegant Data Visualisations Using the Grammar of Graphics, Springer-Verlag New York, 2016. https://ggplot2.tidyverse.org/(accessed February 14, 2023).
|
[28] |
S. Xu, M. Chen, T. Feng, L. Zhan, L. Zhou, G. Yu, Use ggbreak to Effectively Utilize Plotting Space to Deal With Large Datasets and Outliers, Front. Genet. 12(2021) 2122. https://doi.org/10.3389/FGENE.2021.774846/BIBTEX.
|
[29] |
Z. Gu, Complex heatmap visualization, IMeta. 1(2022) e43. https://doi.org/10.1002/imt2.43.
|
[30] |
Z. Gu, R. Eils, M. Schlesner, Complex heatmaps reveal patterns and correlations in multidimensional genomic data, Bioinformatics. 32(2016) 2847-2849. https://doi.org/10.1093/bioinformatics/btw313.
|
[31] |
S. Cajic, R. Hennig, R. Burock, E. Rapp, Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis, NLM (Medline), 2021. https://doi.org/10.1007/978-3-030-76912-3_4.
|
[32] |
S. Cajic, R. Hennig, V. Grote, U. Reichl, E. Rapp, Removable Dyes-The Missing Link for In-Depth N-Glycan Analysis via Multi-Method Approaches, Engineering. 26(2023) 132-150. https://doi.org/10.1016/J.ENG.2023.02.016.
|
[33] |
M. Hilliard, W.R. Alley, C.A. McManus, Y.Q. Yu, S. Hallinan, J. Gebler, P.M. Rudd, Glycan characterization of the NIST RM monoclonal antibody using a total analytical solution:From sample preparation to data analysis, MAbs. 9(2017) 1349-1359. https://doi.org/10.1080/19420862.2017.1377381.
|
[34] |
J. Zhao, W. Peng, X. Dong, Y. Mechref, Analysis of NIST Monoclonal Antibody Reference Material Glycosylation Using the LC-MS/MS-Based Glycoproteomic Approach, J. Proteome Res. 20(2021) 818-830. https://doi.org/10.1021/acs.jproteome.0c00659.
|
[35] |
J.O. Kafader, R.D. Melani, L.F. Schachner, A.N. Ives, S.M. Patrie, N.L. Kelleher, P.D. Compton, Native vs Denatured:An in Depth Investigation of Charge State and Isotope Distributions, J. Am. Soc. Mass Spectrom. 31(2020) 574-581. https://doi.org/10.1021/jasms.9b00040.
|
[36] |
M. Bi, B. Bai, Z. Tian, Structure-Specific N-Glycoproteomics Characterization of NIST Monoclonal Antibody Reference Material 8671, J. Proteome Res. 21(2022) 1276-1284. https://doi.org/10.1021/acs.jproteome.2c00027.
|
[37] |
W. Zhu, M. Li, J. Zhang, Integrating Intact Mass Analysis and Middle-Down Mass Spectrometry Approaches to Effectively Characterize Trastuzumab and Adalimumab Structural Heterogeneity, J. Proteome Res. 20(2021) 270-278. https://doi.org/10.1021/acs.jproteome.0c00373.
|
[38] |
J. Liu, T. Eris, C. Li, S. Cao, S. Kuhns, Assessing Analytical Similarity of Proposed Amgen Biosimilar ABP 501 to Adalimumab, BioDrugs. 30(2016) 321-338. https://doi.org/10.1007/s40259-016-0184-3.
|
[39] |
Y. Yan, A.P. Liu, S. Wang, T.J. Daly, N. Li, Ultrasensitive Characterization of Charge Heterogeneity of Therapeutic Monoclonal Antibodies Using Strong Cation Exchange Chromatography Coupled to Native Mass Spectrometry, Anal. Chem. 90(2018) 13013- 13020. https://doi.org/10.1021/acs.analchem.8b03773.
|
[40] |
O. Montacir, H. Montacir, M. Eravci, A. Springer, S. Hinderlich, A. Saadati, M.K. Parr, Comparability study of Rituximab originator and follow-on biopharmaceutical, J. Pharm. Biomed. Anal. 140(2017) 239-251. https://doi.org/10.1016/j.jpba.2017.03.029.
|
[41] |
B.L. Duivelshof, S. Denorme, K. Sandra, X. Liu, A. Beck, M.A. Lauber, D. Guillarme, V. D'atri, Quantitative N-Glycan Profiling of Therapeutic Monoclonal Antibodies Performed by Middle-Up Level HILIC-HRMS Analysis, Pharmaceutics. 13(2021) 1744. https://doi.org/10.3390/pharmaceutics13111744.
|
[42] |
T. Mouchahoir, J.E. Schiel, Development of an LC-MS/MS peptide mapping protocol for the NISTmAb, Anal. Bioanal. Chem. 410(2018) 2111-2126. https://doi.org/10.1007/s00216-018-0848-6.
|
[43] |
C.-H. Chen, H. Feng, R. Guo, P. Li, A.K.C. Laserna, Y. Ji, B.H. Ng, S.F.Y. Li, S.H. Khan, A. Paulus, S.-M. Chen, A.E. Karger, M. Wenz, D.L. Ferrer, A.F. Huhmer, A. Krupke, Intact NIST monoclonal antibody characterization-Proteoforms, glycoforms-Using CE-MS and CE-LIF, Cogent Chem. 4(2018) 1480455. https://doi.org/10.1080/23312009.2018.1480455.
|
[44] |
C. Grünwald-Gruber, A. Thader, D. Maresch, T. Dalik, F. Altmann, Determination of true ratios of different N-glycan structures in electrospray ionization mass spectrometry, Anal. Bioanal. Chem. 409(2017) 2519-2530. https://doi.org/10.1007/s00216-017-0235- 8.
|
[45] |
K. Stavenhagen, H. Hinneburg, M. Thaysen-Andersen, L. Hartmann, D.V. Silva, J. Fuchser, S. Kaspar, E. Rapp, P.H. Seeberger, D. Kolarich, Quantitative mapping of glycoprotein micro-heterogeneity and macro-heterogeneity:an evaluation of mass spectrometry signal strengths using synthetic peptides and glycopeptides, J. Mass Spectrom. 48(2013) 627-639. https://doi.org/10.1002/JMS.3210.
|
[46] |
T. Čaval, A. Buettner, M. Haberger, D. Reusch, A.J.R. Heck, Discrepancies between High-Resolution Native and Glycopeptide-Centric Mass Spectrometric Approaches:A Case Study into the Glycosylation of Erythropoietin Variants, J. Am. Soc. Mass Spectrom. 32(2021) 2099-2104. https://doi.org/10.1021/jasms.1c00060.
|
[47] |
B. Wang, Y. Tsybovsky, K. Palczewski, M.R. Chance, Reliable determination of site specific in vivo protein N-glycosylation based on collision-induced MS/MS and chromatographic retention time, J. Am. Soc. Mass Spectrom. 25(2014) 729-741. https://doi.org/10.1007/s13361-013-0823-6.
|
[48] |
P. Kozlik, R. Goldman, M. Sanda, Study of structure-dependent chromatographic behavior of glycopeptides using reversed phase nanoLC, Electrophoresis. 38(2017) 2193-2199. https://doi.org/10.1002/elps.201600547.
|
[49] |
F. Di Marco, C. Blöchl, W. Esser-Skala, V. Schäpertöns, T. Zhang, M. Wuhrer, K. Sandra, T. Wohlschlager, C.G. Huber, Glycoproteomics of a single protein:revealing hundreds of thousands of Myozyme® glycoforms by hybrid HPLC-MS approaches, (2022). https://doi.org/10.26434/CHEMRXIV-2022-87TWX.
|
[50] |
R.A. Kerr, D.A. Keire, H. Ye, The impact of standard accelerated stability conditions on antibody higher order structure as assessed by mass spectrometry, MAbs. 11(2019) 930- 941. https://doi.org/10.1080/19420862.2019.1599632.
|
[51] |
L.E. Kilpatrick, E.L. Kilpatrick, Optimizing High-Resolution Mass Spectrometry for the Identification of Low-Abundance Post-Translational Modifications of Intact Proteins, J. Proteome Res. 16(2017) 3255-3265. https://doi.org/10.1021/ACS.JPROTEOME.7B00244/ASSET/IMAGES/LARGE/PR- 2017-00244C_0004.JPEG.
|
[52] |
H. Kaur, Characterization of glycosylation in monoclonal antibodies and its importance in therapeutic antibody development, Crit. Rev. Biotechnol. 41(2021) 300-315. https://doi.org/10.1080/07388551.2020.1869684.
|
[53] |
A.M. Goetze, Y.D. Liu, Z. Zhang, B. Shah, E. Lee, P. V. Bondarenko, G.C. Flynn, Highmannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans, Glycobiology. 21(2011) 949-959. https://doi.org/10.1093/glycob/cwr027.
|
[54] |
M. Yu, D. Brown, C. Reed, S. Chung, J. Lutman, E. Stefanich, A. Wong, J.P. Stephan, R. Bayer, Production, characterization and pharmacokinetic properties of antibodies with N-linked Mannose-5 glycans, MAbs. 4(2012) 475-487. https://doi.org/10.4161/mabs.20737.
|
[55] |
B. Wei, K. Berning, C. Quan, Y.T. Zhang, Glycation of antibodies:Modification, methods and potential effects on biological functions, MAbs. 9(2017) 586-594. https://doi.org/10.1080/19420862.2017.1300214.
|
[56] |
B. Chi, C. Veyssier, T. Kasali, F. Uddin, C.A. Sellick, At-line high throughput sitespecific glycan profiling using targeted mass spectrometry, Biotechnol. Reports. 25(2020) e00424. https://doi.org/10.1016/j.btre.2020.e00424.
|
[57] |
A.R. Hines, M. Edgeworth, P.W.A. Devine, S. Shepherd, N. Chatterton, C. Turner, K.S. Lilley, X. Chen, N.J. Bond, Multi-Attribute Monitoring Method for Process Development of Engineered Antibody for Site-Specific Conjugation, J. Am. Soc. Mass Spectrom. 34(2023) 1330-1341. https://doi.org/10.1021/jasms.3c00037.
|
[58] |
T. Wang, L. Chu, W. Li, K. Lawson, I. Apostol, T. Eris, Application of a Quantitative LC-MS Multiattribute Method for Monitoring Site-Specific Glycan Heterogeneity on a Monoclonal Antibody Containing Two N-Linked Glycosylation Sites, Anal. Chem. 89(2017) 3562-3567. https://doi.org/10.1021/acs.analchem.6b04856.
|
[59] |
S. Luo, B. Zhang, Benchmark Glycan Profile of Therapeutic Monoclonal Antibodies Produced by Mammalian Cell Expression Systems, Pharm. Res. 1(2023) 1-9. https://doi.org/10.1007/s11095-023-03628-4.
|
[60] |
L. Alessandri, D. Ouellette, A. Acquah, M. Rieser, D. LeBlond, M. Saltarelli, C. Radziejewski, T. Fujimori, I. Correia, Increased serum clearance of oligomannose species present on a human IgG1 molecule, MAbs. 4(2012) 509-520. https://doi.org/10.4161/mabs.20450.
|
[61] |
J.E. Huffman, M. Pučić-Baković, L. Klarić, R. Hennig, M.H.J. Selman, F. Vučković, M. Novokmet, J. Krištić, M. Borowiak, T. Muth, O. Polašek, G. Razdorov, O. Gornik, R. Plomp, E. Theodoratou, A.F. Wright, I. Rudan, C. Hayward, H. Campbell, A.M. Deelder, U. Reichl, Y.S. Aulchenko, E. Rapp, M. Wuhrer, G. Lauc, Comparative performance of four methods for high-throughput glycosylation analysis of immunoglobulin G in genetic and epidemiological research, Mol. Cell. Proteomics. 13(2014) 1598-1610. https://doi.org/10.1074/MCP.M113.037465.
|
[62] |
C. Jakes, F. Füssl, I. Zaborowska, J. Bones, Rapid Analysis of Biotherapeutics Using Protein A Chromatography Coupled to Orbitrap Mass Spectrometry, Anal. Chem. (2021). https://doi.org/10.1021/acs.analchem.1c02365.
|
[63] |
E. Largy, F. Cantais, G. Van Vyncht, A. Beck, A. Delobel, Orthogonal liquid chromatography-mass spectrometry methods for the comprehensive characterization of therapeutic glycoproteins, from released glycans to intact protein level, J. Chromatogr. A. 1498(2017) 128-146. https://doi.org/10.1016/j.chroma.2017.02.072.
|
[64] |
M. Li, W. Zhu, H. Zheng, J. Zhang, Efficient HCD-pd-EThcD approach for N-glycan mapping of therapeutic antibodies at intact glycopeptide level, Anal. Chim. Acta. 1189(2022) 339232. https://doi.org/10.1016/j.aca.2021.339232.
|
[65] |
J. Giorgetti, V. D'Atri, J. Canonge, A. Lechner, D. Guillarme, O. Colas, E. WagnerRousset, A. Beck, E. Leize-Wagner, Y.N. François, Monoclonal antibody Nglycosylation profiling using capillary electrophoresis-Mass spectrometry:Assessment and method validation, Talanta. 178(2018) 530-537. https://doi.org/10.1016/j.talanta.2017.09.083.
|
[66] |
K. Groves, A. Cryar, S. Cowen, A.E. Ashcroft, M. Quaglia, Mass Spectrometry Characterization of Higher Order Structural Changes Associated with the Fc-glycan Structure of the NISTmAb Reference Material, RM 8761, J. Am. Soc. Mass Spectrom. 31(2020) 553-564. https://doi.org/10.1021/jasms.9b00022.=
|