An Increase in the Adhesive Ability of Recombinant Spidroins with the Recombinant Adhesive Mussel Foot Protein Mfp3

Abstract

Previously, it was demonstrated that recombinant spidroins rS1/9 and rS2/12 are able to glue various inorganic and organic materials. It is known that mussel foot proteins have unique adhesive properties associated with a high content of L-3,4-dihydroxyphenylalanine (DOPA), which is formed due to modification of tyrosine residues by the enzyme tyrosinase. We constructed a hybrid protein, which contains recombinant mussel foot protein 3 (Mfp3), as well as the recombinant tyrosinase used for modifying the tyrosine residues in DOPA in all recombinant proteins (rS1/9, rS2/12, and Mfp3 in the composition of the hybrid protein). Such modification led to an enhancement of the adhesive properties of these proteins, while the combination of modified spidroins with Mfp3-DOPA significantly increased their adhesive ability, which was demonstrated in the experiments on gluing various materials. The results obtained indicate the high potential of the hybrid protein containing recombinant modified Mfp3 for use alone or as an additive to recombinant spidroins for medical use.