Turning a Killing Mechanism into an Adhesion and Antifouling Advantage

Abstract

Abstract Mild and universal methods to introduce functionality in polymeric surfaces remain a challenge. Herein, a bacterial killing mechanism based on amphiphilic antimicrobial peptides is turned into an adhesion advantage. Surface activity (surfactant) of the antimicrobial liquid chromatography peak I (LCI) peptide is exploited to achieve irreversible binding of a protein–polymer hybrid to surfaces via physical interactions. The protein–polymer hybrid consists of two blocks, a surface‐affine block (LCI) and a functional block to prevent protein fouling on surfaces by grafting antifouling polymers via single electron transfer‐living radical polymerization (SET‐LRP). The mild conditions of SET‐LRP of N ‐2‐hydroxy propyl methacrylamide (HPMA) and carboxybetaine methacrylamide (CBMAA) preserve the secondary structure of the fusion protein. Adsorption kinetics and grafting densities are assessed using surface plasmon resonance and ellipsometry on model gold surfaces, while the functionalization of a range of artificial and natural surfaces, including teeth, is directly observed by confocal microscopy. Notably, the fusion protein modified with poly(HPMA) completely prevents the fouling from human blood plasma and thereby exhibits a resistance to protein fouling that is comparable to the best grafted‐from polymer brushes. This, combined with their simple application on a large variety of materials, highlights the universal and scalable character of the antifouling concept.