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..
[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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[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...
[NMR paper] High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
J Magn Reson. 2014 Apr;241:137-47
Authors: Nucci NV, Valentine KG, Wand AJ
Abstract
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High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids
High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Nathaniel V. Nucci , Kathleen G. Valentine , A. Joshua Wand</br>
High-resolution multi-dimensional solution NMR is unique as a biophysical and biochemical tool in its ability to examine both the structure and dynamics of macromolecules at atomic resolution. Conventional solution NMR approaches, however, are largely limited to examinations of relatively small (<25kDa) molecules,...
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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...
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[NMR paper] High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15299-302
Authors: Wand AJ, Ehrhardt MR, Flynn PF
The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR...
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[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....
Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies
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