Effect of monovalent salts on molecular interactions of globular protein (BSA) above its isoelectric point

Abstract

Protein-protein interactions study is crucial for understanding functions of proteins in the living system. Here, the molecular interactions of bovine serum albumin (BSA) with the addition of different monovalent (Li+, Na+, and K+) and one divalent (Mg2+) cations were studied above the isoelectric point of the protein. Small-angle neutron scattering study reveals that though short-range attractive interactions remain unchanged, long-range repulsion strength decreases with increasing ion concentration. The presence of ions and variation of their concentration also affect the diffusion coefficient of protein. The protein-protein interactions are ion-specific and modified according to the charge density of the cations.