Related ArticlesMolecular 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 with that of excipient molecules based on the spin-lattice relaxation time (T1) of each molecule determined by high resolution 13C solid-state NMR. The relationship between molecular mobility and protein stability is discussed. METHODS: Protein aggregation of lyophilized bovine serum gamma-globulin (BGG) formulation containing dextran was measured by size exclusion chromatography. The T1 of the BGG carbonyl carbon and dextran methin carbon in the formulation was determined by high resolution 13C NMR, and subsequently used to calculate the correlation time (tauc) of each carbon. The spin-spin relaxation time (T2) of BGG and dextran protons was measured by pulsed NMR spectrometry, and the critical temperature of appearance of Lorentzian relaxation due to liquid BGG and dextran protons (Tmc) was determined. RESULTS: The tauc of dextran methin carbon in BGG-dextran formulations exhibited a linear temperature dependence according to the Adam-Gibbs-Vogel equation at lower temperatures, and a nonlinear temperature dependence described by the Vogel-Tamman-Fulcher equation at higher temperatures. The temperature at which molecular motion of dextran changed was consistent with the Tmc. The tauc of BGG carbonyl carbon exhibited a similar temperature dependence to the tauc of the dextran methin carbon and substantially decreased at temperatures above Tmc in the presence of dextran. The temperature dependence of BGG aggregation could be described by the Williams-Landel-Ferry equation even at temperatures 20 degrees C lower than Tmc. CONCLUSIONS: High resolution 13C solid-state NMR indicated that the molecular motion of BGG was enhanced above Tmc in association with the increased global segmental motion of dextran molecules.
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Raquel Godoy-Ruiz, Chenyun Guo and Vitali Tugarinov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1083656/aop/images/medium/ja-2010-083656_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1083656
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hxZ4cabF688
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[NMR paper] A solid-state NMR study of molecular mobility and phase separation in co-spray-dried
A solid-state NMR study of molecular mobility and phase separation in co-spray-dried protein-sugar particles.
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Eur J Pharm Sci. 2005 May;25(1):105-12
Authors: Suihko EJ, Forbes RT, Apperley DC
Molecular mobility and physical form of co-spray-dried sugar-lysozyme formulations were evaluated. Co-spray-dried trehalose:lysozyme and sucrose:lysozyme formulations in 1:9, 1:1 and 9:1 ratios (w:w) were stored at 0% RH and 75%...
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[NMR paper] NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-
NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions.
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Carbohydr Res. 2004 Apr 2;339(5):907-28
Authors: Johnson MA, Pinto BM
Investigations of the conformations of carbohydrates, their analogues and their molecular mimics are described, with emphasis on structural and functional information that can be gained by NMR spectroscopic techniques in combination with molecular...
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[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.
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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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Study of effect of molecular mobility in chromatophore membranes of the bacterium E.
Study of effect of molecular mobility in chromatophore membranes of the bacterium E. shaposhnikovii on processes of photoinduced electron transport using the NMR-spin-echo method with isotope substitution and dehydration.
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Biochemistry (Mosc). 2010 Apr;75(4):423-7
Authors: Chamorovsky CS, Chamorovsky SK, Knox PP
...
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[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...
Molecular mobility of protein in lyophilized formulations linked to the molecular mob
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