Developing biological formulations to maintain the chemical and structural integrity of therapeutic antibodies remains a significant challenge. Monoclonal antibody (mAb) crystalline suspension formulation is a promising alternative for high concentration subcutaneous drug delivery. It demonstrates many merits compared to the solution formulation to reach a high concentration at the reduced viscosity and enhanced stability. One main challenge in drug development is the lack of high-resolution...
[NMR paper] Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations Using (1)H NMR Spectroscopy
Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations Using (1)H NMR Spectroscopy
Biopharmaceutical proteins are important drug therapies in the treatment of a range of diseases. Proteins, such as antibodies (Abs) and peptides, are prone to chemical and physical degradation, particularly at the high concentrations currently sought for subcutaneous injections, and so formulation conditions, including buffers and excipients, must be optimized to minimize such instabilities. Therefore, both the protein and small molecule content of biopharmaceutical...
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03-04-2021 12:41 PM
[NMR paper] Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
J Pharm Sci. 2020 Nov 26;:
Authors: Li M, Koranne S, Fang R, Lu X, Williams DM, Munson EJ, Bhambhani A, Su Y
Abstract
Biophysical and biochemical...
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12-01-2020 11:49 PM
[NMR paper] Investigating protein-ligand interactions by solution NMR spectroscopy.
Investigating protein-ligand interactions by solution NMR spectroscopy.
Investigating protein-ligand interactions by solution NMR spectroscopy.
Chemphyschem. 2018 Jan 04;:
Authors: Becker W, Bhattiprolu KC, Gubensäk N, Zangger K
Abstract
Protein-ligand interactions are of fundamental importance in almost all processes in living organisms. The ligands comprise small molecules, drugs or biological macromolecules and their interaction strength varies over several orders of magnitude. Solution NMR spectroscopy offers a large...
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01-10-2018 12:45 PM
[NMR paper] Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Related Articles Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Inorg Chem. 2017 May 24;
Authors: Bertarello A, Schubeis T, Fuccio C, Ravera E, Fragai M, Parigi G, Emsley L, Pintacuda G, Luchinat C
Abstract
We present the first solid-state NMR study of an iron-sulfur protein. The combined use of very fast (60 kHz) magic-angle spinning and tailored radiofrequency irradiation...
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05-26-2017 08:36 PM
[NMR paper] Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.
Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.
Related Articles Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.
MAbs. 2016 Aug 11;:1-14
Authors: Kheddo P, Cliff MJ, Uddin S, van der Walle CF, Golovanov AP
Abstract
Assessing how excipients affect the self-association of monoclonal antibodies (mAbs) requires informative and direct in situ measurements for highly concentrated solutions, without sample dilution...
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09-03-2016 05:38 PM
Investigating the Structural Dynamics Transitions of Human Adipocyte Fatty Acid Binding Protein by NMR Spectroscopy
Investigating the Structural Dynamics Transitions of Human Adipocyte Fatty Acid Binding Protein by NMR Spectroscopy
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Kim N. Ha , Youlin Xia , Yenchi Tran , Adedolapo Ojoawo , Gianluigi Veglia , David A. Bernlohr</br>
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01-28-2015 05:28 PM
Dynamic nuclear polarization enhanced NMR spectroscopy for pharmaceutical formulations
From The DNP-NMR Blog:
Dynamic nuclear polarization enhanced NMR spectroscopy for pharmaceutical formulations
Rossini, A.J., et al., Dynamic nuclear polarization enhanced NMR spectroscopy for pharmaceutical formulations. J Am Chem Soc, 2014. 136(6): p. 2324-34.
http://www.ncbi.nlm.nih.gov/pubmed/24410528
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03-07-2014 06:47 PM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...