Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions

Winzor, Donald J.; Deszczynski, Marcin; Harding, Stephen E.; Wills, Peter R.

doi:10.1016/j.bpc.2007.03.001

Cited by 62 publications

(89 citation statements)

References 46 publications

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“…Correlation between protein surface coverage and B 22 As described above, the approach using SIC for the determination of The retention volume increases with increasing ionic strength, reflecting changes in B 22 .…”

Section: 1mentioning

confidence: 96%

“…21 Determination of the osmotic second virial coefficient B 22 All mobile phase solutions were buffered with 5 mM acetic acid at pH 3.0 and 4.5 or 5 mM sodium phosphate at pH 6 -8. Lysozyme was dissolved in the studied solutions at 20 mg/ml.…”

Section: Lysozyme Immobilizationmentioning

confidence: 99%

“…Within the framework of the sticky hard sphere model [54], Rosenbaum and colleagues [55,56] showed that the experimentally measured B 22 can be correlated with solubility data [50,[57][58][59][60]. This signifies that short range attractive interactions are the main interactions that describe the phase properties and behavior of a colloidal system [61].…”

mentioning

confidence: 95%

“…A number of different techniques are available for the investigation of protein-protein interactions and protein self-association [17][18][19][20][21][22], however, most techniques lack the possibility being used as a high throughput assay [23][24][25].…”

mentioning

confidence: 99%

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Lysozyme‐lysozyme self‐interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization

Brun¹,

Frieß²,

Schultz-Fademrecht

et al. 2009

Biotechnology Journal

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The purpose of the presented study is to understand the physicochemical properties of proteins in aqueous solutions in order to identify solution conditions with reduced attractive protein‐protein interactions, to avoid the formation of protein aggregates and to increase protein solubility. This is assessed by measuring the osmotic second virial coefficient (B22), a parameter of solution non‐ideality, which is obtained using self‐interaction chromatography. The model protein is lysozyme. The influence of various solution conditions on B22 was investigated: protonation degree, ionic strength, pharmaceutical relevant excipients and combinations thereof. Under acidic solution conditions B22 is positive, favoring protein repulsion. A similar trend is observed for the variation of the NaCl concentration, showing that with increasing the ionic strength protein attraction is more likely. B22 decreases and becomes negative. Thus, solution conditions are obtained favoring attractive protein‐protein interactions. The B22 parameter also reflects, in general, the influence of the salts of the Hofmeister series with regard to their salting‐in/salting‐out effect. It is also shown that B22 correlates with protein solubility as well as physical protein stability.

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Section: 1mentioning

confidence: 96%

Section: Lysozyme Immobilizationmentioning

confidence: 99%

mentioning

confidence: 95%

mentioning

confidence: 99%

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Lysozyme‐lysozyme self‐interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization

Brun¹,

Frieß²,

Schultz-Fademrecht

et al. 2009

Biotechnology Journal

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“…Therefore, the biophysical aspects of mineralization compartments in terms of macromolecular contents as well as the mineralization-dependent chemistry and conformation of additives require attention. Along these lines, experimental design for investigating biomolecular behavior under non-ideal conditions must also consider interactions with small molecules such as buffer components (Winzor et al 2007;Scott et al 2011).…”

Section: Crowded Solutions and Confinement: Impact On Nucleationmentioning

confidence: 99%

Mineralization and non-ideality: on nature’s foundry

Rao¹,

Cölfen

2016

Biophys Rev

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Understanding how ions, ion-clusters and particles behave in non-ideal environments is a fundamental question concerning planetary to atomic scales. For biomineralization phenomena wherein diverse inorganic and organic ingredients are present in biological media, attributing biomaterial composition and structure to the chemistry of singular additives may not provide a holistic view of the underlying mechanisms. Therefore, in this review, we specifically address the consequences of physico-chemical non-ideality on mineral formation. Influences of different forms of non-ideality such as macromolecular crowding, confinement and liquid-like organic phases on mineral nucleation and crystallization in biological environments are presented. Novel prospects for the additive-controlled nucleation and crystallization are accessible from this biophysical view. In this manner, we show that non-ideal conditions significantly affect the form, structure and composition of biogenic and biomimetic minerals.

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Reversible Self‐Association of Pharmaceutical Proteins: Characterization and Case Studies

Sharma¹,

Bajaj

Kalonia

2010

Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals

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Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions

Cited by 62 publications

References 46 publications

Lysozyme‐lysozyme self‐interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization

Lysozyme‐lysozyme self‐interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization

Mineralization and non-ideality: on nature’s foundry

Reversible Self‐Association of Pharmaceutical Proteins: Characterization and Case Studies

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