[NMR paper] Predicting the Stability of Lyophilized Human Serum Albumin Formulations Containing Sucrose and Trehalose Using Solid-State NMR Spectroscopy: Effect of Storage Temperature on (1)H T(1) Relaxation Times
Predicting the Stability of Lyophilized Human Serum Albumin Formulations Containing Sucrose and Trehalose Using Solid-State NMR Spectroscopy: Effect of Storage Temperature on (1)H T(1) Relaxation Times
In a lyophilized protein/disaccharide system, the ability of the disaccharide to form a homogeneous mixture with the protein and to slow the protein mobility dictates the stabilization potential of the formulation. Human serum albumin was lyophilized with sucrose or trehalose in histidine, phosphate, or citrate buffer. ¹H T(1) relaxation times were measured by solid-state NMR spectroscopy...
[NMR paper] Solid-State NMR Characterization of Lyophilized Formulations of Monoclonal Antibody Therapeutics
Solid-State NMR Characterization of Lyophilized Formulations of Monoclonal Antibody Therapeutics
Monoclonal antibodies (mAbs) are an important and growing class of biotherapeutic drugs. Method development for the characterization of critical quality attributes, including higher-order structure (HOS), of mAbs remains an area of active inquiry. Recently, solution-state nuclear magnetic resonance (NMR) spectroscopy has received increased attention and is a means for reliable, high-resolution HOS characterization of aqueous-based preparations of mAbs. While mAbs are predominantly formulated...
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01-27-2023 05:53 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
Probing Functionalities and Acidity of Calcined Phenylene-Bridged Periodic Mesoporous Organosilicates Using (DNP)-NMR, DRIFTS and XPS #DNPNMR
From The DNP-NMR Blog:
Probing Functionalities and Acidity of Calcined Phenylene-Bridged Periodic Mesoporous Organosilicates Using (DNP)-NMR, DRIFTS and XPS #DNPNMR
Pirez, Cyril, Hiroki Nagashima, Franck Dumeignil, and Olivier Lafon. “Probing Functionalities and Acidity of Calcined Phenylene-Bridged Periodic Mesoporous Organosilicates Using (DNP)-NMR, DRIFTS and XPS.” The Journal of Physical Chemistry C, February 19, 2020, acs.jpcc.9b11223.
https://doi.org/10.1021/acs.jpcc.9b11223.
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03-16-2020 04:59 PM
[NMR paper] A solid-state NMR study of protein mobility in lyophilized protein-sugar powders.
A solid-state NMR study of protein mobility in lyophilized protein-sugar powders.
Related Articles A solid-state NMR study of protein mobility in lyophilized protein-sugar powders.
J Pharm Sci. 2002 Apr;91(4):943-51
Authors: Lam YH, Bustami R, Phan T, Chan HK, Separovic F
The molecular mobility of protein in lyophilized lysozyme-sugar systems stored at different relative humidities was studied using solid-state NMR. Relaxation measurements, T(1) of high-frequency (MHz), and T(1rho), of low-frequency (kHz) motions, were performed on lysozyme...
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11-24-2010 08:49 PM
[NMR paper] Molecular mobility of protein in lyophilized formulations linked to the molecular mob
Molecular mobility of protein in lyophilized formulations linked to the molecular mobility of polymer excipients, as determined by high resolution 13C solid-state NMR.
Related Articles Molecular mobility of protein in lyophilized formulations linked to the molecular mobility of polymer excipients, as determined by high resolution 13C solid-state NMR.
Pharm Res. 1999 Oct;16(10):1621-5
Authors: Yoshioka S, Aso Y, Kojima S, Sakurai S, Fujiwara T, Akutsu H
PURPOSE: The mobility of protein molecules in lyophilized protein formulations was compared...