Abstract
Marine and terrestrial organisms often utilise EGF/EGF-like domains in wet adhesives, yet their roles in adhesion remain unclear. Here, we investigate the Barbatia virescense byssal system and uncover an oxidation-independent, reversible, and robust adhesion mechanism where EGF/EGF-like domain tandem repetitions in adhesive proteins bind robustly to GlcNAc-based biopolymer. EGF/EGF-like-domain-containing proteins demonstrate over three-fold superior underwater adhesion to chitosan compared to the well-known strongest wet-adhesive proteins, mefp-5, and suckerin, when adhering to mica in an surface forces apparatus-based measurement. Additionally, as the degree of acetylation of chitosan decreases from 20.0 to 5.34%, the underwater adhesion energy between mefp-2 and chitosan decreases from |Wad | ≈ 41.80 to 12.92 ± 0.40 mJm-2. This finding highlights the importance of GlcNAc over GlcN in binding with EGF to formulate effective underwater adhesives, expanding our understanding of underwater adhesion and supporting EGF's functional role in biomedical wet adhesive interfaces, hydrogels, and chitosan applications.