[NMR paper] Application of Natural Isotopic Abundance (1)H-(13)C- and (1)H-(15)N-Correlated Two-Dimensional NMR for Evaluation of the Structure of Protein Therapeutics.
Application of Natural Isotopic Abundance (1)H-(13)C- and (1)H-(15)N-Correlated Two-Dimensional NMR for Evaluation of the Structure of Protein Therapeutics.
Related ArticlesApplication of Natural Isotopic Abundance (1)H-(13)C- and (1)H-(15)N-Correlated Two-Dimensional NMR for Evaluation of the Structure of Protein Therapeutics.
Methods Enzymol. 2016;566:3-34
Authors: Arbogast LW, Brinson RG, Marino JP
Abstract
Methods for characterizing the higher-order structure of protein therapeutics are in great demand for establishing consistency in drug manufacturing, for detecting drug product variations resulting from modifications in the manufacturing process, and for comparing a biosimilar to an innovator reference product. In principle, solution NMR can provide a robust approach for characterization of the conformation(s) of protein therapeutics in formulation at atomic resolution. However, molecular weight limitations and the perceived need for stable isotope labeling have to date limited its practical applications in the biopharmaceutical industry. Advances in NMR magnet and console technologies, cryogenically cooled probes, and new rapid acquisition methodologies, particularly selective optimized flip-angle short transient pulse schemes and nonuniform sampling, have greatly ameliorated these limitations. Here, we describe experimental methods for the collection and analysis of 2D (1)H(N)-(15)N-amide- and (1)H-(13)C-methyl-correlated spectra applied to protein drug products at natural isotopic abundance, including representatives from the rapidly growing class of monoclonal antibody (mAb) therapeutics. Practical aspects of experimental setup and data acquisition for both standard and rapid acquisition NMR techniques are described. Furthermore, strategies for the statistical comparison of 2D (1)H(N)-(15)N-amide- and (1)H-(13)C-methyl-correlated spectra are detailed.
Natural Abundance (17)O DNP Two-Dimensional and Surface-Enhanced NMR Spectroscopy
From The DNP-NMR Blog:
Natural Abundance (17)O DNP Two-Dimensional and Surface-Enhanced NMR Spectroscopy
Perras, F.A., T. Kobayashi, and M. Pruski, Natural Abundance (17)O DNP Two-Dimensional and Surface-Enhanced NMR Spectroscopy. J Am Chem Soc, 2015. 137(26): p. 8336-9.
http://www.ncbi.nlm.nih.gov/pubmed/26098846
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09-28-2015 06:31 PM
[NMR paper] Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
Anal Chem. 2015 Apr 7;87(7):3556-61
Authors: Arbogast LW, Brinson RG, Marino JP
Abstract
Monoclonal antibodies (mAbs) represent an important and rapidly growing class of biotherapeutics. Correct folding of a mAb is critical for drug efficacy, while misfolding...
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09-19-2015 02:53 PM
Natural Abundance 17O DNP Two-Dimensional and Surface-Enhanced NMR Spectroscopy
Natural Abundance 17O DNP Two-Dimensional and Surface-Enhanced NMR Spectroscopy
Fre?de?ric A. Perras, Takeshi Kobayashi and Marek Pruski
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03905/20150629/images/medium/ja-2015-03905b_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03905
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/2XY9E0YdGEg
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06-29-2015 07:21 PM
Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance
From The DNP-NMR Blog:
Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance
Takahashi, H., S. Hediger, and G. De Paepe, Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance. Chem Commun (Camb), 2013. 49(82): p. 9479-81.
http://www.ncbi.nlm.nih.gov/pubmed/24013616
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11-21-2013 01:14 AM
[NMR paper] Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance.
Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance.
Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance.
Chem Commun (Camb). 2013 Sep 6;
Authors: Takahashi H, Hediger S, De Paëpe G
Abstract
We introduce a general approach for dynamic nuclear polarization (DNP) enhanced solid-state NMR that overcomes the current problems in DNP experiments caused by the use...
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09-10-2013 08:44 PM
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Amy L. Webber, Stefano Masiero, Silvia Pieraccini, Jonathan C. Burley, Andrew S. Tatton, Dinu Iuga, Tran N. Pham, Gian Piero Spada and Steven P. Brown
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206516u/aop/images/medium/ja-2011-06516u_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206516u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
Application of Natural Isotopic Abundance (1)H-(13)C- and (1)H-(15)N-Correlated Two-Dimensional NMR for Evaluation of the Structure of Protein Therapeutics.
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