Polycation-globular protein complex: Ionic strength and chain length effects on the structure and properties

Abstract

The effect of high salt concentration and pH on the binding of globular protein to polycation at different molar masses has been investigated by dynamic light scattering (DLS), turbidimetry and electrostatic modeling for the protein. In dilute concentration regime, DLS and pH titrations showed three remarkable pH transitions: pHc, the pH where soluble complexes of bovine serum albumin (BSA) and linear synthetic Polyethylenemine (PEI) are formed, pHc' presents the end of primary soluble complex and pHφ presents the first appearance of microcoacervate droplets. All pH transitions increase with increasing NaCl concentration. The Adaptive Poisson-Boltzmann Solver (APBS) identify with precision the functional sites at the surface of BSA and shows that the strength of electrostatic interactions depends hugely on the variation of pH and ionic strength. At a very high concentration of salt, no remarkable effect on a mixture formed of a long chain of polycation and globular protein.