Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration

Hill, John J.; Shalaev, Evgenyi; Zografi, George

doi:10.1002/jps.20333

Cited by 95 publications

(87 citation statements)

References 293 publications

(274 reference statements)

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“…These conditions can be numerous, and freeze-drying is well known to be one of them [5][6][7]. When the protein does not refold back to its native state after reconstitution, its activity might be reduced or absent.…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopy and multivariate analysis for the rapid discrimination between native-like and non-native states in freeze-dried protein formulations

Pieters

Heyden

Roger³

et al. 2013

European Journal of Pharmaceutics and Biopharmaceutics

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Section: Introductionmentioning

confidence: 99%

Raman spectroscopy and multivariate analysis for the rapid discrimination between native-like and non-native states in freeze-dried protein formulations

Pieters

Heyden

Roger³

et al. 2013

European Journal of Pharmaceutics and Biopharmaceutics

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“…Broad thermal softening transitions have been seen in calorimetric studies of lysozyme, hemoglobin and myoglobin (Sartor and The arrows indicate the dynamic transition region of the curve (Hill et al, 2005) .…”

Section: Motions In Proteinsmentioning

confidence: 95%

“…Another possibility is that this break reflects a glass-like transition within the amorphous dry protein (Hill, Shalaev, & Zografi, 2005). Hydrated globular proteins undergo a dynamical transition (Td) at 200 K, a phenomenon well documented by X-ray diffraction analysis of thermal B-factors (Rasmussen, Stock, Ringe, & Petsko, 1992), neutron scattering (Cusack, 1989;Cusack, Smith, Finney, Tidor, & Karplus, 1988;Doster, Cusack, & Petry, 1990;Loncharich & Brooks, 1990;, and differential scanning calorimetry (Barkalov, Bol'shakov, Gol'danskii, & Krupyanskii, 1992).…”

Section: Matrix Molecular Mobilitymentioning

confidence: 99%

“…Above T d , dynamic behavior is dominated by highly temperature dependent, large-scale, anharmonic, collective motions of bonded and non-bonded atoms superimposed on small amplitude vibrational motions, whereas below T d , nearly small-amplitude, harmonic vibrations exist with a temperature dependence similar to the harmonic atomic vibrations in small molecule crystals" (Hill et al, 2005). Broad thermal softening transitions have been seen in calorimetric studies of lysozyme, hemoglobin and myoglobin (Sartor and The arrows indicate the dynamic transition region of the curve (Hill et al, 2005) .…”

Section: Motions In Proteinsmentioning

confidence: 99%

“…Due to its similarity to the high-temperature dynamical transition seen in small molecules and polymers, this transition is often referred to as a glass transition (Ringe & Petsko, 2003). Although it is not known whether Td is modulated by water in a manner comparable to Tg, Td does appear to increase considerably upon dehydration (Hill et al, 2005).…”

Section: Matrix Molecular Mobilitymentioning

confidence: 99%

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Molecular mobility and oxygen permeability in amorphous β-lactoglobulin films

Sundaresan

Ludescher

2008

Food Hydrocolloids

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OF THE DISSERTATIONOur overall objective is to understand how molecular mobility modulates diffusion rates and thus chemical reactivity in films made from amorphous β-lactoglobulin. The phosphorescence emission spectra and lifetimes of the triplet probe erythrosin B embedded in the β-Lg films provide measures of the modes, rates, and distribution of molecular mobility in the film, providing the molecular detail necessary to connect food quality and stability to molecular structure and mobility. The mobility contours generated from this research provided us with information about the onset temperature and level of molecular mobility required to support permeability of atmospheric oxygen. In β-Lgbased binary matrices, sugars (sucrose, trehalose, maltose), plasticizers (glycerol, sorbitol, maltitol and PEG-400), fatty acids (palmitic acid, caprylic acid) and protein (BSA) were selected to investigate how variations in composition influence the molecular mobility and oxygen permeability in amorphous β-Lg matrix. Further more complicated β-Lg -based ternary matrices (maltose and maltitol) and (PEG and sucrose) were generated inorder to gain a deeper understanding of edible films.iii In pure β-Lg films there was linear correlation between molecular mobility and oxygen permeability. Various additives showed different results with respect to mobility and permeability. The addition of sucrose, maltose, maltitol and trehalose greatly reduced the mobility and the permeability of the β-Lg matrix. Glycerol exhibited an antiplasticization effect and showed decreased mobility at a molar ratio of 1:1 glycerol/ β-Lg.PEG greatly enhanced the permeability of β-Lg matrix. Fatty acids palmitic acid and caprylic acid had a rigidification effect on the matrix with no change in permeability. We were able to detect dynamic synergies in β-Lg maltose and maltitol mixtures, whereby these sugar-polyol mixtures at equal ratios anti-plasticized the β-Lg matrix and at unequal ratios plasticized the matrix. The tertiary matrix comprising of β-Lg, PEG 400and sucrose brought about a substantial reduction in the permeability. A better understanding of the mobility in these complex matrices will help improve the effectiveness of β-Lg in barrier applications in real food systems.

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Process Development of Protein Therapeutics

Thomas

Guhan

Pettit

2010

Burger's Medicinal Chemistry and Drug Discovery

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The application of recombinant DNA technology to the production of protein therapeutics has undergone considerable progress since first introduced 30 years ago. Considerable scientific effort has been devoted to developing robust processes that produce large amounts of complex proteins with the desired product quality attributes. An overview of the contributions from the four major disciplines working in concert to deliver these processes and methods will be covered. This chapter will discuss some of the tools, methods, and approaches used to produce, purify, formulate, and analyze the drugs of modern biotechnology. Future trends in each of the disciplines will also be presented.

show abstract

Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration

Cited by 95 publications

References 293 publications

Raman spectroscopy and multivariate analysis for the rapid discrimination between native-like and non-native states in freeze-dried protein formulations

Raman spectroscopy and multivariate analysis for the rapid discrimination between native-like and non-native states in freeze-dried protein formulations

Molecular mobility and oxygen permeability in amorphous β-lactoglobulin films

Process Development of Protein Therapeutics

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