Interaction between β-Lactoglobuline and Weak Polyelectrolyte Chains: A Study Using Monte Carlo Simulation

TORRES, PAOLA; EVELINA QUIROGA; ANTONIO JOSÉ RAMIREZ-PASTOR; BOERIS, VALERIA; CLAUDIO NARAMBUENA

JOURNAL OF PHYSICAL CHEMISTRY B - (Print)

AMER CHEMICAL SOC

Lugar: Washington; Año: 2019

1520-6106

Complexation between the β-lactoglobulin and a weak acid polyelectrolyte has beenstudied using Monte Carlo simulations. Different coarse-grained models were used to represent the system and two different acidic constants were used on the PE model. The protein-PE interaction is quantified considering the average PE monomers adsorbed on the protein as function of pH. It was found a maximum in the interaction between macromolecules, which is explained as a function of the titration behavior of the β-lactoglobuline and weak PE. We also found that there was a direct relation between the pH range of monomers adsorbed and the change on dissociation profile of the protein and weak PE compared to isolated conditions. The complexation of protein-PE increased both the dissociation degree of the PE chain and the protein net charge. This benefits the monomers adsorption on the protein surface.