Development of Bioadhesives Based on Recombinant Analogues of Spider Web Proteins

Abstract

It has been shown that the recombinant spidroins rS1/9 and rS2/12, which were developed by us previously, exhibit adhesive properties with respect to both inorganic and organic substrates. It is well known that the adhesive properties of mussel leg proteins are associated with the level of L-3,4-dihydroxy-phenylalanine (DOPA), which is formed as a result of the post-translational modification of tyrosine residues by the tyrosinase enzyme. Therefore, we used recombinant tyrosinase for in vitro modification of tyrosine residues in the recombinant rS1/9 and rS2/12 spidroins to increase their adhesion capacity. The conversion of tyrosine residues into DOPA led to an increase in the adhesion properties of these proteins, which was demonstrated in experiments on gluing plates of polyvinyl chloride, aluminum, polylactic acid, and also tubular pork bones. The molecules of recombinant spidroins retained their inherent properties to form supramolecular structures, hydrogels (microgels), transparent films and 3D matrices. Interestingly, tyrosinase-modified proteins exhibited increased cohesion in experiments on bonding different materials in the presence of water. recombinant spidroins, modification, tyrosinase, DOPA, wetting, adhesion, cohesion The work was supported by a state assignment no. АААА-А20-120093090015-2.