Tailoring the hydrophilicity of solid surfaces with a strong affinity to water has been extensively explored in the last 20 years, but studies have been limited to the single function of wettability. Here, the multifunctional properties of tailored surface films are extended from exhibiting superwettability to facilitating biological activities. It is shown that amyloid fibrils can be universally coated onto various substrates, such as fabrics (non-woven organic masks), metal meshes, polyethersulfone (PES), glass, and more, endowing the resulting surfaces with excellent performance in oil/water mixture and emulsion separation, antifouling, and antifogging. Moreover, the biocompatible crosslinked amyloid fibril coatings can serve as a platform for biocatalytic activities by immobilizing enzymes, as shown in the 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) oxidation and Reactive Black 5 (RB5) degradation by laccase from Trametes versicolor. The study provides a universal approach to modifying surface morphology and chemical properties via fibrous protein templates, opening the way to unexplored bio-based applications and functionalities.
Keywords: amyloid fibrils; antifogging; antifouling; enzyme immobilization; oil/water separation; β-lactoglobulin.
© 2022 The Authors. Advanced Materials published by Wiley-VCH GmbH.