[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] 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
Journal Highlight: Assessment of higher order structure comparability in ... - spectroscopyNOW.com
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Journal Highlight: Assessment of higher order structure comparability in ...
spectroscopyNOW.com
Abstract: In this work, we applied nuclear magnetic resonance (NMR) spectroscopy to rapidly assess higher order structure (HOS) comparability in protein samples. Using a variation of the NMR fingerprinting approach described by Panjwani et al.
Journal Highlight: Assessment of higher order structure comparability in ... - spectroscopyNOW.com
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06-03-2013 04:21 PM
Journal Highlight: Assessment of higher order structure comparability in therapeutic proteins using nuclear magnetic resonance spectroscopy
Journal Highlight: Assessment of higher order structure comparability in therapeutic proteins using nuclear magnetic resonance spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/13ef9b3d882.jpgNMR spectroscopy using a fingerprinting approach has been used to rapidly assess higher order structure comparability in three nonglycosylated proteins spanning a molecular weight range of 6.5–67 kDa.
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06-03-2013 04:21 PM
[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....
Biosimilar structural comparability assessment by NMR: from small proteins to monoclonal antibodies - Nature.com
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