Relevant Properties for Immobilizing Short Peptides on Biosurfaces

Understanding protein and oligopeptide adsorption on biomaterial surfaces is important to develop new biomaterials with improved properties. The phenomenon of peptide adsorption is determined by many parameters such environmental pH, surface topographical features, surface polarity, peptide structure, and/or surface and peptide electric charges. We assessed the effect of surface and peptide net charges on oligopeptide adsorption on synthetic surfaces under different conditions. We have also assessed the ability of immobilizing peptides on the surface generating covalent bonds or electrostatic attraction. Direct relation between the amount of peptide adsorbed on the surface and the difference in net charge between surface and peptides was determined. No relation between the difference in net charge and the ability to promote covalent bonds between peptide and surface was found. Competitive adsorption experiments confirmed these findings. Understanding the specific interactions during adsorption of peptides onto synthetic surfaces improves our ability to develop strategies for the efficient immobilization of oligopeptides on biomaterial surfaces.