CONCLUSION: The chemometric analyses support the lack of statistical differences in the structure of pH-thermal stressed adalimumab, however, it reveals conformational changes or chemical modifications in trastuzumab after forced degradation. Application of chemometrics in comparative NMR studies enables HOS characterization and showcases the sensitivity and specificity in detecting differences in the spectra of mAbs after pH-thermal forced degradation with respect to local and global protein...
[NMR paper] Unambiguous identification of ?-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy
Unambiguous identification of ?-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy
The ?-Gal epitope consisting of the terminal trisaccharide Gal?1,3Gal?1,4GlcNAc exposed on cell or protein surfaces can cause severe immune reactions, such as hypersensitivity reactions, in humans. This epitope is also called the xenotransplantation epitope because it is one of the main reasons for the rejection of non-human organ transplants by the human innate immune response. Recombinant therapeutic proteins expressed in murine cell lines may contain ?-Gal epitopes, and therefore their...
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10-16-2022 03:12 AM
[NMR paper] Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies
Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies
CONCLUSION: Fab-Fab or Fab-Fc interactions may lead to formation of protein networks at high concentration. The early transients to these network formation may be manifested through peak broadening or peak shift in the 2D NMR spectrum of mAb/mAb fragments. Such insights go beyond rank ordering mAbs based on viscosity behavior, which can be obtained by other methods as well..
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02-18-2022 12:50 PM
[NMR paper] Quantification of natural abundance NMR data differentiates the solution behavior of monoclonal antibodies and their fragments
Quantification of natural abundance NMR data differentiates the solution behavior of monoclonal antibodies and their fragments
Biotherapeutics are an important class of molecules for the treatment of a wide range of diseases. They include low molecular weight peptides, highly engineered protein scaffolds and monoclonal antibodies. During their discovery and development, assessments of the biophysical attributes is critical to understanding the solution behavior of therapeutic proteins and for de-risking liabilities. Thus, methods that can quantify, characterize, and provide a basis to...
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10-07-2021 03:03 AM
[NMR paper] Biosimilar structural comparability assessment by NMR: from small proteins to monoclonal antibodies.
Biosimilar structural comparability assessment by NMR: from small proteins to monoclonal antibodies.
Related Articles Biosimilar structural comparability assessment by NMR: from small proteins to monoclonal antibodies.
Sci Rep. 2016;6:32201
Authors: Japelj B, Ilc G, Maruši? J, Sen?ar J, Kuzman D, Plavec J
Abstract
Biosimilar drug products must have a demonstrated similarity with respect to the reference product's molecules in order to ensure both the effectiveness of the drug and the patients' safety. In this paper the fusion...
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09-01-2016 07:21 PM
[NMR paper] 2D (1)H(N), (15)N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies.
2D (1)H(N), (15)N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies.
Related Articles 2D (1)H(N), (15)N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies.
Pharm Res. 2015 Oct 9;
Authors: Arbogast LW, Brinson RG, Formolo T, Hoopes JT, Marino JP
Abstract
PURPOSE: High-resolution nuclear magnetic resonance spectroscopy (NMR) provides a robust approach for producing unique...
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10-12-2015 01:04 AM
[NMR paper] Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Anal Chem. 2013 Sep 5;
Authors: Poppe L, Jordan JB, Lawson K, Jerums M, Apostol I, Schnier PD
Abstract
Nuclear magnetic resonance (NMR) is arguably the most direct methodology for characterizing the higher-order structure of proteins in solution. Structural characterization of proteins by NMR typically utilizes heteronuclear experiments. However, for formulated monoclonal antibody (mAb) therapeutics, the...
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09-07-2013 09:54 PM
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Abstract 1H NMR (nuclear magnetic resonance spectroscopy) has been used for metabolomic analysis of â??Rieslingâ?? and â??Mueller-Thurgauâ?? white wines from the German Palatinate region. Diverse two-dimensional NMR techniques have been applied for the identification of metabolites, including phenolics. It is shown that sensory analysis correlates with NMR-based metabolic profiles of wine. 1H NMR data in combination...
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03-03-2011 02:06 AM
[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
Application of NMR and Chemometric Analyses to Better Understand the Quality Attributes in pH and Thermally Degraded Monoclonal Antibodies
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