Self-assembled peptides on polymer surfaces: towards morphology-dependent surface functionalization

Abstract

A bi-functional peptide with polymer-binding and antifouling capabilities was designed as a polymer-surface modifier. The binding of the peptide onto the target polymer surface and the subsequent protein adsorption were analyzed quantitatively. The amount of peptide immobilized on the polymer surface regulated the nanometer-sized morphologies with variable peptidyl secondary structures, followed by drastic changes in the fouling versus antifouling properties.