Adhesion and Wettability of Marine Adhesive Proteins in Aqueous Systems

Abstract

Abstract The work of adhesion on substrates with low and high surface energies using a variety of homo, random and sequential polypeptides containing L-lysine has been investigated to evaluate the role of individual amino acids together with the sequences in marine adhesive proteins. The work of adhesion of poly (L-lysine) was lower (34–79 mJ/m2) on the surfaces of Teflon and polyethylene (PE) with low energy, and was higher (108 mJ/m2) on the surface of glass with high energy, and the order was glass > nylon > polyethylene > Teflon. The work of adhesion increased with the increasing amount of the Tyr residues, and Lys copolypeptides were always larger than Glu copolypeptides. Among sequential polypeptides, polypeptides containing Gly and Lys exhibited higher work of adhesion on four different substrates, suggesting the important role of Gly and Lys residues in the adhesive proteins. Biological adhesion of a goby fish sperm on the glass plate exhibited marked adhesion activity due to the lysyl residues in the precoated marine adhesive proteins.