(99j) Interfacial Protein Self-Assembly: An "Ironic" Approach Towards Generating Antifouling Coatings

Non-specific adsorption of proteins, also known as fouling, is a “common but very complicated phenomenon” hallmarked by its ubiquity. Most research aims to prevent fouling, which can be detrimental to the function of devices, such as biosensors and membranes, and can promote harmful pathologies, such as antibiotic-resistant infections. Rather than regarding fouling as a persistent problem, our work leverages the non-specific interactions of silk fibroin during self-assembly to form stable and substrate-tolerant thin-film coatings. These coatings provide complete surface coverage and can grow to tens of nanometers thick, transforming the physicochemical properties of a surface in a one-pot aqueous process without requiring substrate pre-activation or covalent chemistries. Our studies have demonstrated that silk fibroin coatings can be formed on a variety of substrates ranging from hydrophobic Teflon to hydrophilic TiO₂. Furthermore, these coatings can exhibit beneficial properties for resisting the adhesion of gram negative and gram positive bacteria. Our research moreover delves into the complex interplay of surface-protein and protein-protein interactions underlying coating formation to establish methods by which we can tune the coating process.