Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions

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Abstract

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.
Lingua originaleEnglish
pagine (da-a)11829-11836
Numero di pagine8
RivistaJOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Volume116
Stato di pubblicazionePublished - 2012

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All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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