Interaction of Myoglobin colloids with BSA in solution: Insights into complex formation and elastic compliance

This work focusses on the supramolecular complex formed between Myoglobin (Mb) and Bovine Serum Albumin (BSA) at colloids/solution interface at pH 4.0 and pH 7.5. Electrostatic interactions between Mb as colloids and BSA solution (pH=7.5 and 4.0) have been confirmed by Zeta potential that suggest that while Mb has a narrow interaction range, BSA has a wider interaction space. The organization of Mb colloids in BSA characterized using dilational rheological parameters show that the Mb colloids are elastic and the strong adsorbed water layers on the surface restrict the deformation, regulated by the viscoelastic surface layer. Stability of the complexes analyzed using UV-vis, Fluorescence and Circular dichroic spectroscopy indicate that there is a 1:1 interaction between Mb and BSA with a binding constant of about 10⁵M^-1. Quartz Crystal microbalance with dissipation has been used to evaluate the elastic compliance of the complexes of Mb colloids dispersed in very dilute BSA solution. The higher elastic compliance at pH=4.0 (than at pH=7.5) and the complex sizes correlate with changes in zeta potential suggesting that the mechanical properties of the protein in colloids are dependent on both the electrostatic interaction as well as the degree of hydration of the colloids.