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RESEARCH PRODUCT
Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions
Antonio EmanueleMassimo PanzicaLorenzo Cordonesubject
SucroseSucrosechemistry.chemical_compoundDynamic light scatteringMaterials ChemistryAnimalsTransition TemperaturePhysical and Theoretical ChemistryBovine serum albuminProtein Structure QuaternarySugarChromatographyAqueous solutionbiologyTemperatureTrehaloseWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsSolutionsSolventtrehalose protein aggregation solvent effects light scatteringchemistrySolventsbiology.proteinCattleProtein MultimerizationSolvent effectsdescription
We report results of static and dynamic light scattering measurements performed on bovine serum albumin (BSA) in saccharide (trehalose and sucrose) solutions. Our aim is to study the effects of the two disaccharides on the first steps of thermal aggregation of BSA in aqueous solutions at two protein concentrations (1 and 30 mg/mL) at increasing sugar/water ratio. Results show that sugars modify early stages of aggregation mainly by perturbing the thermodynamic behavior of the solvent (i.e., general solvent effects) without involving direct, specific sugar-protein interactions. This agrees with current hypotheses on sugar action in protein solutions. (1-3) The linear correlation detected between the characteristic temperature of the aggregation process and the glass transition temperature of the water-sugar solvent strengthens the above suggestions.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-09-21 | The Journal of Physical Chemistry B |