Adsorption characteristics of oligopeptides composed of acidic and basic amino acids on titanium surface

The adsorption characteristics of octapeptides, containing different numbers of aspartic acid, lysine, and alanine residues (i.e., D₄K₀A₄, D₄K₁A₃, D₄K₃A₁, D₄K₄A₀, and D₀K₄A₄) on the surface of titanium (Ti) particles were investigated in the pH range of 3.0-8.8 at 30°C. The adsorption isotherms for octapeptides having four plural aspartic acid residues with or without lysine residues showed two distinct adsorption modes, i.e., irreversible and reversible modes, at pHs 3.0-6.5; at pH 7.0 or higher, the adsorption mode was reversible. Increasing the number of lysine residues at a fixed number of aspartic acid residues (i.e., 4) decreased the amount of peptides adsorbed in both modes. D₄K₄A₀ adsorbed irreversibly at pHs 3.0-6.5, due to the fact that negatively charged carboxyl groups directly interact with a positively charged Ti surface, whereas positively charged amino groups of lysine residues are directed in an opposite direction toward the solution side, as predicted by molecular mechanics/dynamics calculations.