[NMR paper] Comparative Analysis of 1D PROFILE and 2D 1H,13C Methyl NMR Methods for Characterization of the Higher Order Structure of IgG1 Monoclonal Antibodies.
Related ArticlesComparative Analysis of 1D PROFILE and 2D 1H,13C Methyl NMR Methods for Characterization of the Higher Order Structure of IgG1 Monoclonal Antibodies.
Anal Chem. 2020 Apr 08;:
Authors: Elliott KW, Ghasriani H, Wikstrom M, Giddens JP, Aubin Y, Delaglio F, Marino JP, Arbogast L
Abstract
The use of NMR spectroscopy has emerged as a premier tool to characterize the higher order structure of protein therapeutics and in particular IgG1 monoclonal antibodies (mAbs). Due to their large size, traditional 1H-15N correlation experiments have proven exceedingly difficult to implement on mAbs and a number of alternative techniques have been proposed, including the 1D 1H PROFILE method and the 2D 1H-13C methyl correlation based approach. Both 1D and 2D approaches have relative strengths and weaknesses, related to the inherent sensitivity and resolution of the respective methods. To further increase the utility of NMR to the biopharmaceutical community, harmonized criteria for decision making in employing 1D and 2D approaches for mAb characterization is warranted. To this end, we have conducted an interlaboratory comparative study of the 1D-PROFILE and 2D-Methyl methods on several mAbs samples to determine the degree to which each method is suited to detect spectral difference between the samples and the degree to which results from each correlate with one another. Results from the study demonstrate both methods provide statistical data highly comparable to one another and that each method is capable of complementing the limitations commonly associated with the other, thus providing a better overall picture of higher order structure.
PMID: 32267681 [PubMed - as supplied by publisher]
Quality assessment of biologics: higher order structure analysis using NMR - European Pharmaceutical Review
Quality assessment of biologics: higher order structure analysis using NMR European Pharmaceutical ReviewThe webinar will describe how 2D NMR can offer protein biochemists unprecedented analytical precision. By assigning just one spectrum, users can obtain a ...
Quality assessment of biologics: higher order structure analysis using NMR - European Pharmaceutical Review
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[NMR paper] Effect of Polysorbate 20 and Polysorbate 80 on the Higher Order Structure of a Monoclonal Antibody and its Fab and Fc Fragments Probed Using 2D NMR.
Effect of Polysorbate 20 and Polysorbate 80 on the Higher Order Structure of a Monoclonal Antibody and its Fab and Fc Fragments Probed Using 2D NMR.
Effect of Polysorbate 20 and Polysorbate 80 on the Higher Order Structure of a Monoclonal Antibody and its Fab and Fc Fragments Probed Using 2D NMR.
J Pharm Sci. 2017 Aug 23;:
Authors: Singh SM, Bandi S, Jones DNM, Mallela KMG
Abstract
We examined how polysorbate 20 (PS20; Tween 20) and polysorbate 80 (PS80; Tween 80) affect the higher order structure of a monoclonal antibody (mAb)...
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08-28-2017 10:59 AM
[NMR paper] Simple NMR methods for evaluating higher order structures of monoclonal antibody therapeutics with quinary structure.
Simple NMR methods for evaluating higher order structures of monoclonal antibody therapeutics with quinary structure.
Related Articles Simple NMR methods for evaluating higher order structures of monoclonal antibody therapeutics with quinary structure.
J Pharm Biomed Anal. 2016 Jun 7;128:398-407
Authors: Chen K, Long DS, Lute SC, Levy MJ, Brorson KA, Keire DA
Abstract
Monoclonal antibody (mAb) drugs constitute the largest class of protein therapeutics currently on the market. Correctly folded protein higher order structure...
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06-28-2016 06:25 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...
[NMR paper] On the Analytical Superiority of 1D NMR for Fingerprinting the Higher Order Structure of Protein Therapeutics Compared to Multidimensional NMR Methods.
On the Analytical Superiority of 1D NMR for Fingerprinting the Higher Order Structure of Protein Therapeutics Compared to Multidimensional NMR Methods.
Related Articles On the Analytical Superiority of 1D NMR for Fingerprinting the Higher Order Structure of Protein Therapeutics Compared to Multidimensional NMR Methods.
Anal Chem. 2015 Apr 30;
Authors: Poppe L, Jordan JB, Rogers G, Schnier PD
Abstract
An important aspect in the analytical characterization of protein therapeutics is the comprehensive characterization of higher...
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05-02-2015 09:41 PM
Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy
From The DNP-NMR Blog:
Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy
Debelouchina, G.T., et al., Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy. J Am Chem Soc, 2013. 135(51): p. 19237-47.
http://www.ncbi.nlm.nih.gov/pubmed/24304221
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[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...
Comparative Analysis of 1D PROFILE and 2D 1H,13C Methyl NMR Methods for Characterization of the Higher Order Structure of IgG1 Monoclonal Antibodies.
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