Effect of hydrophobic groups on adsorption of arginine-based amino acids to solid surfaces in water

Abstract

We calculate the free energies of adsorption between a solid wall and various arginine derivatives in water using molecular dynamics simulations. We vary the hydrophobic group size of the amino acids in two ways and the hydrophilicity of the solid wall in five ways. The free energy of adsorption decreases by increasing the hydrophilicity of the solid wall, regardless of the size of the hydrophobic group. Amino acids with small hydrophobic groups are adsorbed on the solid wall with the strongest hydrophilicity, but the free energy of the amino acids with large hydrophobic groups is relatively small. The free energy of adsorption in benzene solvent is increased by increasing the hydrophilicity of the solid wall; however, analogous to results in water solvent, it is independent of the size of the hydrophobic group. We attribute these differences in free energy to the effect of solvent molecules localized on the solid wall. Thus, these results may modulate peptide adsorption on a solid surface by the size of the peptide’s hydrophobic groups.