Interaction between potassium iodide and bovine serum albumin, ovalbumin and lysozyme under different temperature induction.

In this study, the interaction between potassium iodide and protein molecules under different temperature induction was studied, taking potassium iodide (KI) and protein molecules as a model system. The effects of KI on protein conformation, size, surface charge, binding constant, and binding site were analyzed by fluorescence spectrum, infrared spectrum, and diffusing wave spectroscopy. The results revealed that bovine serum albumin (BSA)/ovalbumin (OVA) and I formed the 1: 1 complex and significantly affected the hydrodynamic radius and spatial structure. This could be attributed to the exposure of tyrosine residues inside the proteins to the polar conditions under increased temperature. The unfolding of protein structures induced the interaction between KI/KCl and proteins. As for BSA and OVA, the particle size and surface charge of the complex increased significantly in the presence of KI/KCl. KI had a strong static quenching effect on the fluorescence of BSA and OVA. Overall, these results provide insights into the physiological effects of iodine ions.