[NMR paper] Predicting the Stability of Formulations Containing Lyophilized Human Serum Albumin and Sucrose/Trehalose Using Solid-State NMR Spectroscopy
Stabilization of proteins by disaccharides in lyophilized formulations depends on the interactions between the protein and the disaccharide (system homogeneity) and the sufficiently low mobility of the system. Human serum albumin (HSA) was lyophilized with disaccharides (sucrose and/or trehalose) in different relative concentrations. Solid-state nuclear magnetic resonance (ssNMR) spectroscopy ¹H T(1) and ¹H T(1?) relaxation times were measured to determine the homogeneity of the lyophilized...
[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...
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[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
[NMR paper] Study of interaction of human serum albumin with curcumin by NMR and docking.
Study of interaction of human serum albumin with curcumin by NMR and docking.
Study of interaction of human serum albumin with curcumin by NMR and docking.
J Mol Model. 2014 Aug;20(8):2365
Authors: Singh DV, Bharti SK, Agarwal S, Roy R, Misra K
Abstract
Curcumin has been reported to be therapeutically active but has poor bioavailability, half life, and high rate of metabolic detoxifcation. Most of the hydrophobic and acidic drugs get transported through human serum albumin (HSA). Binding of drugs to serum protein increases their...
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07-18-2014 01:02 PM
[NMR paper] Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mn(II) binding to human serum albumin: a ¹H-NMR relaxometric study.
J Inorg Biochem. 2012 Dec;117:198-203
Authors: Fanali G, Cao Y, Ascenzi P, Fasano M
Abstract
Human serum albumin (HSA) displays several metal binding sites, participating to essential and toxic metal ions disposal and transport. The major Zn(II) binding site,...
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09-27-2013 03:28 AM
[NMR paper] Determination of molecular mobility of lyophilized bovine serum albumin and gamma-glo
Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Related Articles Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Pharm Res. 1996 Jun;13(6):926-30
Authors: Yoshioka S, Aso Y, Kojima S
PURPOSE: Feasibility of solid-state 1H NMR for determining the mobility of protein molecules in lyophilized cakes was considered. The mobility in...
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08-22-2010 02:27 PM
[NMR paper] The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and
The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.
J Pharm Biomed Anal. 1995 Aug;13(9):1087-93
Authors: Bertucci C, Ascoli G, Uccello-Barretta G, Di Bari L, Salvadori P
5-Fluorouracil (FU) is an important and widely used antineoplastic drug...
Predicting the Stability of Formulations Containing Lyophilized Human Serum Albumin and Sucrose/Trehalose Using Solid-State NMR Spectroscopy
Linear Mode
