The success of modern biopharmaceutical products depends on enhancing the stability of protein therapeutics. Freezing and thawing, which are common thermal stresses encountered throughout the lifecycle of drug substances, spanning protein production, formulation design, manufacturing, storage, and shipping, can impact this stability. Understanding the physicochemical and molecular behaviors of components in biological drug products at temperatures relevant to manufacturing and shipping is...
[NMR paper] Supramolecular Protein-Polyelectrolyte Assembly at Near Physiological Conditions-Water Proton NMR, ITC, and DLS Study
Supramolecular Protein-Polyelectrolyte Assembly at Near Physiological Conditions-Water Proton NMR, ITC, and DLS Study
The in vivo potency of polyphosphazene immunoadjuvants is inherently linked to the ability of these ionic macromolecules to assemble with antigenic proteins in aqueous solutions and form physiologically stable supramolecular complexes. Therefore, in-depth knowledge of interactions in this biologically relevant system is a prerequisite for a better understanding of mechanism of immunoadjuvant activity. Present study explores a self-assembly of polyphosphazene...
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[NMR paper] Investigating Crystalline Protein Suspension Formulations of Pembrolizumab from MAS NMR Spectroscopy
Investigating Crystalline Protein Suspension Formulations of Pembrolizumab from MAS NMR Spectroscopy
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...
Study of electron spectral diffusion process under DNP conditions by ELDOR spectroscopy focusing on the 14N Solid Effect #DNPNMR
From The DNP-NMR Blog:
Study of electron spectral diffusion process under DNP conditions by ELDOR spectroscopy focusing on the 14N Solid Effect #DNPNMR
Ramirez Cohen, Marie, Akiva Feintuch, Daniella Goldfarb, and Shimon Vega. “Study of Electron Spectral Diffusion Process under DNP Conditions by ELDOR Spectroscopy Focusing on the 14N Solid Effect.” Magnetic Resonance Discussions, February 24, 2020, 1–26.
https://doi.org/10.5194/mr-2020-3.
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Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the...
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[NMR paper] Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Related Articles Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Proc Natl Acad Sci U S A. 2018 Apr 16;:
Authors: Charlier C, Alderson TR, Courtney JM, Ying J, Anfinrud P, Bax A
Abstract
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded...
Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab
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