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21. Protocols for the analytical characterization of therapeutic monoclonal antibodies. I – Non-denaturing chromatographic techniques B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Goyon, Alexandre; D’Atri, Valentina; Bobaly, Balazs; Wagner-Rousset, Elsa; Fekete, Szabolcs; Guillarme, Davy;     Show all 7 Authors
Source:
Journal of chromatography 2017 v.1058 pp. 73-84
ISSN:
1570-0232
Subject:
Food and Drug Administration; biopharmaceuticals; gel chromatography; hydrophobic interaction chromatography; hydrophobicity; immune response; ion exchange chromatography; isoelectric point; molecular weight; monoclonal antibodies; proteins; standard operating procedures
Abstract:
... Size-, charge- and hydrophobicity-related variants of a biopharmaceutical product have to be deeply characterized for batch consistency and for the assessment of immunogenicity and safety effects. Size exclusion chromatography (SEC) and ion exchange chromatography (IEX) are considered as the gold standard for the analysis of high molecular weight species (HMWS) and charge-related variants, respect ...
DOI:
10.1016/j.jchromb.2017.05.010

22. Evaluation of size exclusion chromatography columns packed with sub-3μm particles for the analysis of biopharmaceutical proteins A

Author:
Beck, Alain,   et al.   ; Goyon, Alexandre; Colas, Olivier; Sandra, Koen; Guillarme, Davy; Fekete, Szabolcs;     Show all 6 Authors
Source:
Journal of chromatography 2017 v.1498 pp. 80-89
ISSN:
0021-9673
Subject:
biopharmaceuticals; electrostatic interactions; gel chromatography; hydrophobic bonding; hydrophobicity; models; monoclonal antibodies; plate count; proteins
Abstract:
... The aim of this study was to evaluate the practical possibilities and limitations of several recently introduced size exclusion chromatographic (SEC) columns of 150×4.6mm, sub–3μm (Agilent AdvanceBioSEC 2.7μm, Tosoh TSKgel UP-SW3000 2.0μm, Phenomenex Yarra SEC X-150 1.8μm and Waters Acquity BEH200 1.7μm) for the separation of biopharmaceutical proteins. For this purpose, some model proteins were t ...
DOI:
10.1016/j.chroma.2016.11.056

23. Orthogonal liquid chromatography–mass spectrometry methods for the comprehensive characterization of therapeutic glycoproteins, from released glycans to intact protein level

Author:
Beck, Alain,   et al.   ; Largy, Eric; Cantais, Fabrice; Van Vyncht, Géry; Delobel, Arnaud;     Show all 5 Authors
Source:
Journal of chromatography 2017 v.1498 pp. 128-146
ISSN:
0021-9673
Subject:
polysaccharides; glycosylation; biopharmaceuticals; hydrophilic interaction chromatography; therapeutics; capillary electrophoresis; computer software; mass spectrometry; glycoproteins
Abstract:
... Proteins are increasingly used as therapeutics. Their characterization is challenging due to their size and inherent heterogeneity notably caused by post-translational modifications, among which glycosylation is probably the most prominent. The glycosylation profile of therapeutic proteins must therefore be thoroughly analyzed. Here, we illustrate how the use of a combination of various cutting-ed ...
DOI:
10.1016/j.chroma.2017.02.072

24. Top-down and middle-down approach by fraction collection enrichment using off-line capillary electrophoresis – mass spectrometry coupling: Application to monoclonal antibody Fc/2 charge variants A

Author:
Beck, Alain,   et al.   ; Biacchi, Michael; Said, Nassur; Leize-Wagner, Emmanuelle; François, Yannis-Nicolas;     Show all 5 Authors
Source:
Journal of chromatography 2017 v.1498 pp. 120-127
ISSN:
0021-9673
Subject:
biopharmaceuticals; capillary electrophoresis; chromatography; mass spectrometry; monoclonal antibodies; proteins
Abstract:
... The characterization of complex protein mixtures represents one of the biggest challenge in many research fields such as biological or biopharmaceutical sciences. Out of all categories, monoclonal antibodies (mAbs) and related products drawn the most interest due to their strong therapeutic potency and specificity. Because of their intrinsic complexity due to a large number of micro-heterogeneitie ...
DOI:
10.1016/j.chroma.2017.02.064

25. Characterization of therapeutic antibodies and related products by two-dimensional liquid chromatography coupled with UV absorbance and mass spectrometric detection B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Stoll, Dwight; Danforth, John; Zhang, Kelly;     Show all 4 Authors
Source:
Journal of chromatography 2016 v.1032 pp. 51-60
ISSN:
1570-0232
Subject:
absorbance; drug formulations; glycosylation; ion exchange; liquid chromatography; mass spectrometry; monoclonal antibodies; proteins
Abstract:
... The development of analytical tools for the characterization of large biomolecules is an emerging and rapidly evolving area. This development activity is motivated largely by the current trend involving the increase in development and use of large biomolecules for therapeutic uses. Given the inherent complexity of these biomolecules, which arises from their sheer size and possibilities for chemica ...
DOI:
10.1016/j.jchromb.2016.05.029

26. Cutting-edge capillary electrophoresis characterization of monoclonal antibodies and related products B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Gahoual, Rabah; Leize-Wagner, Emmanuelle; François, Yannis-Nicolas;     Show all 4 Authors
Source:
Journal of chromatography 2016 v.1032 pp. 61-78
ISSN:
1570-0232
Subject:
biopharmaceuticals; capillary zone electrophoresis; chromatography; isoelectric focusing; mass spectrometry; monoclonal antibodies; proteins
Abstract:
... Out of all categories, monoclonal antibodies (mAbs), biosimilar, antibody-drug conjugates (ADCs) and Fc-fusion proteins attract the most interest due to their strong therapeutic potency and specificity. Because of their intrinsic complexity due to a large number of micro-heterogeneities, there is a crucial need of analytical methods to provide comprehensive in-depth characterization of these molec ...
DOI:
10.1016/j.jchromb.2016.05.028

27. Independent highly sensitive characterization of asparagine deamidation and aspartic acid isomerization by sheathless CZE‐ESI‐MS/MS

Author:
Beck, Alain,   et al.   ; Gahoual, Rabah; François, Yannis‐Nicolas; Leize‐Wagner, Emmanuelle;     Show all 4 Authors
Source:
Journal of mass spectrometry 2016 v.51 no.2 pp. 150-158
ISSN:
1076-5174
Subject:
asparagine; aspartic acid; capillary zone electrophoresis; deamidation; electrospray ionization mass spectrometry; ionization; isomerization; monoclonal antibodies; pH; post-translational modification; protein structure; synthetic peptides; temperature
Abstract:
... Amino acids residues are commonly submitted to various physicochemical modifications occurring at physiological pH and temperature. Post‐translational modifications (PTMs) require comprehensive characterization because of their major influence on protein structure and involvement in numerous in vivo process or signaling. Mass spectrometry (MS) has gradually become an analytical tool of choice to c ...
DOI:
10.1002/jms.3735

28. Development of a fast workflow to screen the charge variants of therapeutic antibodies A

Author:
Beck, Alain,   et al.   ; Wagner-Rousset, Elsa; Fekete, Szabolcs; Morel-Chevillet, Laura; Colas, Olivier; Corvaïa, Nathalie; Cianférani, Sarah; Guillarme, Davy;     Show all 8 Authors
Source:
Journal of chromatography 2017 v.1498 pp. 147-154
ISSN:
0021-9673
Subject:
cation exchange chromatography; drug therapy; drugs; immunoglobulin G; monitoring; monoclonal antibodies; peptide mapping; research and development; risk
Abstract:
... Chemical or enzymatic modifications of therapeutic monoclonal antibodies (mAbs) having high risk towards safety and efficacy are defined as critical quality attributes (CQAs). During therapeutic mAbs process development, a variety of analytical techniques have to be used for the thorough characterization and quantitative monitoring of CQAs. This paper describes the development of a rapid analytica ...
DOI:
10.1016/j.chroma.2017.02.065

29. Top-down analysis of immunoglobulin G isotypes 1 and 2 with electron transfer dissociation on a high-field Orbitrap mass spectrometer

Author:
Beck, Alain,   et al.   ; Fornelli, Luca; Ayoub, Daniel; Aizikov, Konstantin; Liu, Xiaowen; Damoc, Eugen; Pevzner, Pavel A.; Makarov, Alexander; Tsybin, Yury O.;     Show all 9 Authors
Source:
Journal of proteomics 2017 v.159 pp. 67-76
ISSN:
1874-3919
Subject:
dissociation; electron transfer; energy; gases; immunoglobulin G; ions; mass spectrometry; monoclonal antibodies; polypeptides; spectrometers
Abstract:
... The increasing importance of immunoglobulins G (IgGs) as biotherapeutics calls for improved structural characterization methods designed for these large (~150kDa) macromolecules. Analysis workflows have to be rapid, robust, and require minimal sample preparation. In a previous work we showed the potential of Orbitrap Fourier transform mass spectrometry (FTMS) combined with electron transfer dissoc ...
DOI:
10.1016/j.jprot.2017.02.013
PubMed:
28242452
PubMed Central:
PMC5478168

30. Multiplexed Middle-Down Mass Spectrometry as a Method for Revealing Light and Heavy Chain Connectivity in a Monoclonal Antibody

Author:
Beck, Alain,   et al.   ; Srzentić, Kristina; Nagornov, Konstantin O.; Fornelli, Luca; Lobas, Anna A.; Ayoub, Daniel; Kozhinov, Anton N.; Gasilova, Natalia; Menin, Laure; Gorshkov, Mikhail V.; Aizikov, Konstantin; Tsybin, Yury O.;     Show all 12 Authors
Source:
Analytical chemistry 2018 v.90 no.21 pp. 12527-12535
ISSN:
1520-6882
Subject:
absorption; drugs; ions; liquid chromatography; monoclonal antibodies; myoglobin; proteomics; sequence analysis; signal-to-noise ratio; spectrometers; tandem mass spectrometry; therapeutics
Abstract:
... Pairing light and heavy chains in monoclonal antibodies (mAbs) using top-down (TD) or middle-down (MD) mass spectrometry (MS) may complement the sequence information on single chains provided by high-throughput genomic sequencing and bottom-up proteomics, favoring the rational selection of drug candidates. The 50 kDa F(ab) subunits of mAbs are the smallest structural units that contain the require ...
DOI:
10.1021/acs.analchem.8b02398

31. Systematic evaluation of mobile phase additives for the LC–MS characterization of therapeutic proteins

Author:
Beck, Alain,   et al.   ; Bobály, Balázs; Fekete, Jenő; Guillarme, Davy; Fekete, Szabolcs;     Show all 5 Authors
Source:
Talanta 2015 v.136 pp. 60-67
ISSN:
0039-9140
Subject:
additives; biopharmaceuticals; buffers; formates; mass spectrometry; molecular weight; pH; proteins; reversed-phase liquid chromatography
Abstract:
... Trifluoroacetic acid (TFA) is commonly used as mobile phase additive for the analysis of proteins in reversed phase liquid chromatography (RPLC). Due to its interesting features, it provides symmetrical and narrow peak shapes for proteins, but decreases mass spectrometric sensitivity through ion-pairing and spray destabilizing. Since RPLC–MS is an important technique for the characterization of pr ...
DOI:
10.1016/j.talanta.2014.12.006

32. Adsorption and recovery issues of recombinant monoclonal antibodies in reversed‐phase liquid chromatography†

Author:
Beck, Alain,   et al.   ; Fekete, Szabolcs; Wagner, Elsa; Vuignier, Karine; Guillarme, Davy;     Show all 5 Authors
Source:
Journal of separation science 2015 v.38 no.1 pp. 1-8
ISSN:
1615-9306
Subject:
adsorption; ferritin; glycosylation; human serum albumin; hydrophobicity; immunoglobulin G; isoelectric point; molecular weight; monoclonal antibodies; ovalbumin; reversed-phase liquid chromatography; silica; transferrin
Abstract:
... The poor recovery of large biomolecules is a well‐known issue in reversed‐phase liquid chromatography. Several papers have reported this problem, but the reasons behind this behavior are not yet fully understood. In the present study, state‐of‐the‐art reversed‐phase wide‐pore stationary phases were used to evaluate the adsorption of therapeutic monoclonal antibodies. These biomolecules possess mol ...
DOI:
10.1002/jssc.201400996

33. Analysis of antibody-drug conjugates by comprehensive on-line two-dimensional hydrophobic interaction chromatography x reversed phase liquid chromatography hyphenated to high resolution mass spectrometry. II- Identification of sub-units for the characterization of even and odd load drug species B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Sarrut, Morgan; Fekete, Szabolcs; Janin-Bussat, Marie-Claire; Colas, Olivier; Guillarme, Davy; Heinisch, Sabine;     Show all 7 Authors
Source:
Journal of chromatography 2016 v.1032 pp. 91-102
ISSN:
1570-0232
Subject:
drugs; hydrophobic interaction chromatography; isomers; mass spectrometry; reversed-phase liquid chromatography
Abstract:
... This paper is the second part of a two-part series dedicated to the development of an on-line comprehensive HICxRPLC-UV/MS method for the characterization of a commercial inter-chain cysteine-linked ADC (brentuximab vedotin, Adcetris®). The first part focused on the optimization of the chromatographic conditions. In the second part of this series of papers, the structural characterization of the B ...
DOI:
10.1016/j.jchromb.2016.06.049

34. Potential of hydrophilic interaction chromatography for the analytical characterization of protein biopharmaceuticals A

Author:
Beck, Alain,   et al.   ; Periat, Aurélie; Fekete, Szabolcs; Cusumano, Alessandra; Veuthey, Jean-Luc; Lauber, Matthew; Guillarme, Davy;     Show all 7 Authors
Source:
Journal of chromatography 2016 v.1448 pp. 81-92
ISSN:
0021-9673
Subject:
adsorption; biopharmaceuticals; hydrophilic interaction chromatography; interferon-alpha; ligands; silica; temperature; viscosity
Abstract:
... A new stationary phase based on wide-pore hybrid silica bonded with amide ligand has been used to explore the utility of HILIC for the analytical characterization of protein biopharmaceuticals. Various, highly-relevant samples were tested, including different insulins, interferon α-2b and trastuzumab. This work shows that HILIC can be successfully employed for the analysis of therapeutic proteins ...
DOI:
10.1016/j.chroma.2016.04.056

35. Structural characterization of antibody drug conjugate by a combination of intact, middle-up and bottom-up techniques using sheathless capillary electrophoresis – Tandem mass spectrometry as nanoESI infusion platform and separation method

Author:
Beck, Alain,   et al.   ; Said, Nassur; Gahoual, Rabah; Kuhn, Lauriane; François, Yannis-Nicolas; Leize-Wagner, Emmanuelle;     Show all 6 Authors
Source:
Analytica chimica acta 2016 v.918 pp. 50-59
ISSN:
0003-2670
Subject:
analytical chemistry; biogeography; capillary electrophoresis; data collection; drugs; glycosylation; hydrophobicity; monoclonal antibodies; peptides; proteolysis; tandem mass spectrometry
Abstract:
... Antibody-drug conjugates (ADCs) represent a fast growing class of biotherapeutic products. Their production leads to a distribution of species exhibiting different number of conjugated drugs overlaying the inherent complexity resulting from the monoclonal antibody format, such as glycoforms. ADCs require an additional level of characterization compared to first generation of biotherapeutics obtain ...
DOI:
10.1016/j.aca.2016.03.006

36. Characterization of cetuximab Fc/2 dimers by off-line CZE-MS

Author:
Beck, Alain,   et al.   ; François, Yannis-Nicolas; Biacchi, Michael; Said, Nassur; Renard, Charly; Gahoual, Rabah; Leize-Wagner, Emmanuelle;     Show all 7 Authors
Source:
Analytica chimica acta 2016 v.908 pp. 168-176
ISSN:
0003-2670
Subject:
analytical chemistry; chemical structure; drugs; glycosylation; lysine; mass spectrometry; molecular weight; monoclonal antibodies; pH; therapeutics
Abstract:
... Monoclonal antibody (mAb) therapeutics attract the largest concern due to their strong therapeutic potency and specificity. The Fc region of mAbs is common to many new biotherapeutics as biosimilar, antibody drug conjugate or fusion protein. Fc region has consequences for Fc-mediated effector functions that might be desirable for therapeutic applications. As a consequence, there is a continuous ne ...
DOI:
10.1016/j.aca.2015.12.033

37. On-Chip Mesoporous Functionalized Magnetic Microspheres for Protein Sequencing by Extended Bottom-up Mass Spectrometry

Author:
Beck, Alain,   et al.   ; Gasilova, Natalia; Srzentić, Kristina; Qiao, Liang; Liu, Baohong; Tsybin, Yury O.; Girault, Hubert H.;     Show all 7 Authors
Source:
Analytical chemistry 2016 v.88 no.3 pp. 1775-1784
ISSN:
1520-6882
Subject:
aspartic proteinases; cost effectiveness; fractionation; high-throughput nucleotide sequencing; hydrophobicity; magnetic fields; mass spectrometry; monoclonal antibodies; peptides; porous media; proteolysis; proteomics; sequence homology
Abstract:
... A limited amount and extreme concentration variability of proteomic-related samples require efficient analyte preconcentration and purification prior to the mass spectrometry (MS)-based analysis. Preferably, these steps should be coupled online with chosen fractionation and detection techniques for the minimization of the sample loss. To realize such sample pretreatment, herein, an on-chip solid-p ...
DOI:
10.1021/acs.analchem.5b04045

38. Analysis of antibody-drug conjugates by comprehensive on-line two-dimensional hydrophobic interaction chromatography x reversed phase liquid chromatography hyphenated to high resolution mass spectrometry. I − Optimization of separation conditions B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Sarrut, Morgan; Corgier, Amélie; Fekete, Szabolcs; Guillarme, Davy; Lascoux, David; Janin-Bussat, Marie-Claire; Heinisch, Sabine;     Show all 8 Authors
Source:
Journal of chromatography 2016 v.1032 pp. 103-111
ISSN:
1570-0232
Subject:
drugs; hydrophobic interaction chromatography; manufacturing; mass spectrometry; mixing; quality control; reversed-phase liquid chromatography; solvents
Abstract:
... Antibody-drug-conjugates (ADCs) manufacturing leads to a mixture of species which needs to be characterized during development and for further quality control. The coupling of on-line HIC x RPLC to high resolution mass spectrometry can be considered as a very efficient analytical method, providing extensive information on ADC sample, within a reduced time scale. Our intention in this first paper i ...
DOI:
10.1016/j.jchromb.2016.06.048

39. A new anti-human Fc method to capture and analyze ADCs for characterization of drug distribution and the drug-to-antibody ratio in serum from pre-clinical species B Analytical technologies in the biomedical and life sciences

Author:
Beck, Alain,   et al.   ; Excoffier, Mélissa; Janin-Bussat, Marie-Claire; Beau-Larvor, Charlotte; Troncy, Lysiane; Corvaia, Nathalie; Klinguer-Hamour, Christine;     Show all 7 Authors
Source:
Journal of chromatography 2016 v.1032 pp. 149-154
ISSN:
1570-0232
Subject:
Macaca fascicularis; antibody specificity; antigens; biotin; blood serum; clinical trials; drugs; enzyme-linked immunosorbent assay; humans; ligands; liquid chromatography; mass spectrometry; mice; monoclonal antibodies; neoplasm cells; patients; precipitin tests; rats; therapeutics; toxicity
Abstract:
... Antibody-drug conjugates (ADCs) are becoming a major class of oncology therapeutics. They combine monoclonal antibody specificity for over-expressed tumor antigens and the high cytoxicity of small molecular drugs (SMDs) and can therefore selectively kill tumor cells while minimizing toxicity to normal cells. Nevertheless, the premature deconjugation of ADCs in the circulation may trigger off targe ...
DOI:
10.1016/j.jchromb.2016.05.037

40. Direct Identification of Rituximab Main Isoforms and Subunit Analysis by Online Selective Comprehensive Two-Dimensional Liquid Chromatography–Mass Spectrometry

Author:
Beck, Alain,   et al.   ; Stoll, Dwight R.; Harmes, David C.; Danforth, John; Wagner, Elsa; Guillarme, Davy; Fekete, Szabolcs;     Show all 7 Authors
Source:
Analytical chemistry 2015 v.87 no.16 pp. 8307-8315
ISSN:
1520-6882
Subject:
cation exchange chromatography; comprehensive two-dimensional liquid chromatography; mass spectrometry; monoclonal antibodies; reversed-phase liquid chromatography
Abstract:
... In this proof-of-concept study, rituximab, which is a reference therapeutic monoclonal antibody (mAb), was characterized through the implementation of online, selective comprehensive two-dimensional liquid chromatography (sLC×LC) coupled with mass spectrometry (MS), using a middle-up approach. In this setup, cation exchange chromatography (CEX) and reverse-phase liquid chromatography (RPLC) were u ...
DOI:
10.1021/acs.analchem.5b01578