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

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.

Automated summary

This study investigates the molecular interactions between bovine serum albumin (BSA) and different monovalent and one divalent cations. The findings reveal that the strength of long-range repulsion decreases with increasing ion concentration, while short-range attractive interactions remain unaffected. The presence and concentration of ions also impact the protein's diffusion coefficient. The protein-protein interactions are specific to the type of ions and are modified based on their charge density.