We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repulsion favours the disordered non-specific interactions between molecules and consequently affects the aggregation rate. Finally, the comparison between BSA and another relative protein, HSA, allows us to clarify the role of different domains involved in the aggregation process.

Vetri, V., Librizzi, F., Leone, M., Militello, V. (2007). Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 36, 717-725 [10.1007/s00249-007-0196-5].

Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin

VETRI, Valeria;LIBRIZZI, Fabio;LEONE, Maurizio;MILITELLO, Valeria
2007-01-01

Abstract

We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repulsion favours the disordered non-specific interactions between molecules and consequently affects the aggregation rate. Finally, the comparison between BSA and another relative protein, HSA, allows us to clarify the role of different domains involved in the aggregation process.
Vetri, V., Librizzi, F., Leone, M., Militello, V. (2007). Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 36, 717-725 [10.1007/s00249-007-0196-5].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10447/8254
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