Abstract
To study the changes in secondary, tertiary and quaternary structures and the alteration in protein–protein interactions during the protein aggregation upon heating, bovine serum albumin (BSA) was incubated over a range of temperature, and its structure was monitored by various biophysical techniques including circular dichroism (CD), second-derivative UV absorption spectroscopy, dynamic light scattering (DLS) and size exclusion chromatography coupled with multiangle laser light scattering (SEC-MALLS). The experimental data demonstrated that the size of BSA was relatively stable up to 60 °C. Above 65 °C, however, BSA underwent the obvious heat-induced aggregation (a dramatic growth of hydrodynamic radius R h), accompanied with great unfolding of its secondary structure (a sigmoidal reduction of α-helix with the transition midpoint at 67.6 °C), with significant expansion of its tertiary structure (an increased solvent exposure of some aromatic residues with the transition midpoint at 65.5 °C), with distinct screening of electrostatic repulsion (a great reduction of second virial coefficient A 2 above 65 °C) and with remarkable formation of aggregates (an evident increase of molecular weight above 65 °C).
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