Toward Protein-Repellent Surface Coatings from Catechol-Containing Cationic Poly(2-ethyl-2-oxazoline).

Area of Science:

• Biomaterials Science
• Polymer Chemistry
• Surface Science

Background:

• Mussel adhesive proteins inspire novel surface modification strategies.
• Protein fouling is a significant challenge in biomedical and industrial applications.
• Developing robust, protein-repellent surfaces is crucial for preventing unwanted biological interactions.

Purpose of the Study:

• To design and synthesize novel protein-repellent macromolecules.
• To investigate the surface binding properties and film-forming capabilities of these polymers.
• To evaluate the antifouling performance of the developed coatings against model proteins.

Main Methods:

• Copolymerization of poly(2-ethyl-2-oxazoline) with a catechol-containing monomer.
• Introduction of cationic groups via partial acidic hydrolysis.
• Surface affinity analysis using quartz crystal microbalance with dissipation monitoring (QCM-D).
• Assessment of protein attachment inhibition using model proteins like BSA, fibrinogen, and lysozyme.

Main Results:

• Polymers with catechol units demonstrated strong surface binding to diverse substrates (gold, iron, borosilicate, polystyrene).
• Cationic functionalization enabled the formation of defined, durable polymer films, unlike neutral counterparts.
• The developed coatings effectively prevented the attachment of model proteins, showcasing significant nonfouling properties.

Conclusions:

• A novel platform for creating biomimetic, protein-repellent surfaces has been successfully developed.
• The combination of catechol and cationic groups in polyoxazoline chains provides controlled surface adhesion and robust antifouling characteristics.
• This approach offers a versatile and straightforward method for fabricating nonfouling coatings for various applications.