LAUSR

Inspired by mussel proteins that enable surface binding in harsh marine environments, we envisioned a platform of protein-repellent macromolecules based on poly(2-ethyl-2-oxazoline) carrying catechol and cationic functional groups. To facilitate surface attachment, catechol units were installed by copolymerizing a functional comonomer, i.e., 2-(3,4-dimethoxyphenyl)-2-oxazoline, in a gradient fashion. Cationic units were introduced by partial acidic hydrolysis. The surface affinity of these polymers was probed using a quartz crystal microbalance with dissipation monitoring (QCM-D), and it was found that polymers with catechol units had a strong tendency to form surface-bound layers on different substrates, i.e., gold, iron, borosilicate, and polystyrene. While the neutral catechol-containing polymers showed strong, but uncontrolled binding, the ones with additional cationic units were able to form defined and durable polymer films. These coatings were able to prevent the attachment of different model proteins, i.e., bovine serum albumin (BSA), fibrinogen (FI), or lysozyme (LYZ). The herein-introduced platform offers straightforward access to nonfouling surface coatings using a biomimetic approach.