Current Pharmaceutical Biotechnology

Zeno Foldes-Papp
Visiting Professor of Medical Biochemistry
HELIOS Clinical Center of Emergency Medicine
Department for Internal Medicine
Alte-Koelner-Strasse 9
D-51688 Koeln-Wipperfuerth
Germany

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Colloidal Behavior of Proteins: Effects of the Second Virial Coefficient on Solubility, Crystallization and Aggregation of Proteins in Aqueous Solution

Author(s): Joseph J. Valente, Robert W. Payne, Mark C. Manning, W. W. Wilson and Charles S. Henry

Affiliation: Legacy BioDesign, 1826Monarch Circle, Loveland, CO 80538, USA;

Abstract:

There has been an increasing awareness that proteins, like other biopolymers, are large enough to exhibit colloidal behavior in aqueous solution. Net attractive or repulsive forces have been found to govern important physical properties, such as solubility and aggregation. The extent of intermolecular interactions, usually expressed in terms of the osmotic second virial coefficient, B, is most often measured using static light scattering. More recently, self-interaction chromatography (SIC) has emerged as a method for rapid determination of B in actual formulations, as it uses much less protein and has higher throughput. This review will summarize the relationship of B to crystallization, solubility, and aggregation of proteins in aqueous solution. Moreover, the capability of SIC to obtain B values in a rapid and reproducible fashion will be described in detail. Finally, the use of miniaturized devices to measure B is presented.

Keywords: Second virial coefficient, B values, self-interaction chromatography, protein aggregation, protein solubility, protein crystallization

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Article Details

VOLUME: 6
ISSUE: 6
Page: [427 - 436]
Pages: 10
DOI: 10.2174/138920105775159313
Price: $58