Lysozyme-lysozyme self-interactions as assessed by the osmotic second virial coefficient: impact for physical protein stabilization
| Autor: | Patrick Garidel, Wolfgang Friess, Silke Muehlau, Virginie Le Brun, Torsten Schultz-Fademrecht |
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| Rok vydání: | 2009 |
| Předmět: |
Chromatography
Aqueous solution Binding Sites Hofmeister series Thermodynamics Protonation General Medicine Protein aggregation Applied Microbiology and Biotechnology chemistry.chemical_compound chemistry Virial coefficient Models Chemical Ionic strength Osmotic Pressure Molecular Medicine Computer Simulation Muramidase Lysozyme Protein stabilization Algorithms Protein Binding |
| Zdroj: | Biotechnology journal. 4(9) |
| ISSN: | 1860-7314 |
| Popis: | 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 (B(22)), 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 B(22) was investigated: protonation degree, ionic strength, pharmaceutical relevant excipients and combinations thereof. Under acidic solution conditions B(22) 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. B(22) decreases and becomes negative. Thus, solution conditions are obtained favoring attractive protein-protein interactions. The B(22) 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 B(22) correlates with protein solubility as well as physical protein stability. |
| Databáze: | OpenAIRE |
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