Recombinant Antifreeze Protein Type I as a Potential Peptide-Based Anti-Fouling Material for Biomedical Surfaces

Anti-fouling of material surfaces is a major concern in the performance of biomedical materials in biological environments. Surface modification of polymeric materials is an effective strategy for controlling the anti-fouling properties of biomedical materials. Synthetic polymers such as poly(ethylene glycol) (PEG), which exhibit high bioinertness and anti-fouling properties, are widely used. Peptide-based anti-fouling materials are gaining attention because of their biocompatibility, long-term biodegradability, and structural diversity. In this study, we explored the potential of antifreeze protein type I (AFP) from winter flounder as a peptide-based anti-fouling material. AFP possesses a simple α-helical structure of approximately 30 amino acid residues and presents an amphiphilic interface consisting of an ice-binding surface and a hydrophilic surface. We constructed a recombinant AFP that can be modified on a glass substrate and evaluated its anti-fouling properties. The AFP-modified substrates significantly suppressed the adsorption of plasma proteins, such as human albumin, fibrinogen, and fibronectin. Furthermore, adhesion of human ovarian cancer SKOV3 cells and mouse platelets to the substrates was suppressed by AFP modification. Notably, tandem-repeat AFP constructs exhibited high resistance to proteolytic enzymes, such as trypsin. These findings highlight the potential of recombinant AFP as a potential peptide-based anti-fouling material for biomedical applications.