Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level Interactions

• Published in: Journal of solution chemistry 2017-04, Vol.46 (4), p.831-848
• Main Authors: Satish, Lakkoji, Millan, Sabera, Das, Satyabrata, Jena, Sarita, Sahoo, Harekrushna
• Format: Article
• Language: English
• Subjects: Agglomeration; Albumins; Binding sites; Buffer solutions; Chemistry; Chemistry and Materials Science; Condensed Matter Physics; Destabilization; Dichroism; Fluorescence; Geochemistry; Imidazole; Industrial Chemistry/Chemical Engineering; Inorganic Chemistry; Molecular docking; Morphology; Oceanography; Photon correlation spectroscopy; Physical Chemistry; Proteins; Serum albumin; Sodium phosphate
• ISSN: 0095-9782; 1572-8927
• DOI: 10.1007/s10953-017-0612-0

We have studied the effect of some conventional buffers, which are used frequently for biological research, on the thermal aggregation behavior of bovine serum albumin (BSA). The aggregation kinetics of BSA in buffer solutions were investigated by using UV–Vis spectroscopy. The buffers include sodium phosphate buffer, TRIS buffer and imidazole buffer at physiological pH (7.4). Dynamic light scattering and scanning electron microscopy have been employed to illustrate the size and morphology of protein aggregates. The molecular level interactions of buffer molecules with BSA was probed by various spectroscopic techniques, including UV–Vis, fluorescence, and circular dichroism. The results of this study reveal that the strong interactions of the buffers with protein’s folded/unfolded structures lead to stabilization/destabilization of BSA. We have also explored the possible binding sites of BSA for these buffers using a molecular docking technique.