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

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6 Citazioni (Scopus)

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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Trehalose
sucrose
Sugar (sucrose)
sugars
Bovine Serum Albumin
albumins
Sugars
serums
Sucrose
Agglomeration
aqueous solutions
proteins
Proteins
Water
Disaccharides
carbohydrates
Dynamic light scattering
glass transition temperature
water
suggestion

All Science Journal Classification (ASJC) codes

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

Cita questo

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title = "Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions",
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.",
keywords = "trehalose, protein aggregation, solvent effects, light scattering",
author = "Lorenzo Cordone and Antonio Emanuele and Massimo Panzica",
year = "2012",
language = "English",
volume = "116",
pages = "11829--11836",
journal = "Journal of Physical Chemistry B",
issn = "1520-6106",
publisher = "American Chemical Society",

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TY - JOUR

T1 - Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions

AU - Cordone, Lorenzo

AU - Emanuele, Antonio

AU - Panzica, Massimo

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - trehalose, protein aggregation, solvent effects, light scattering

UR - http://hdl.handle.net/10447/66239

M3 - Article

VL - 116

SP - 11829

EP - 11836

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

SN - 1520-6106

ER -