Influence of sodium periodate and tyrosinase on binding of alginate to adlayers of mytilus edulis foot protein 1

Abstract

Mytilus edulis foot protein 1 (Mefp-1) is the most well-characterized component of this sea mussel's adhesive plaque. The plaque is a condensed, heterogeneous mixture consisting of a large proportion of cross-linked biopolymers that bonds the mussel to a chosen mooring. Mefp-1 is densely populated with lysine and L-3,4-dihyroxyphenylalanine (L-dopa) residues incorporated into a repeating amino acid sequence motif. It has been proposed that one plaque cross-linking reaction is the nucleophilic addition of the ϵ-amino groups of the lysine residues into the oxidized catechol (o-diphenol) functionality (quinone) of the L-dopa residues. In order to determine if this reaction occurs in adlayers of Mefp-1, a previously developed assay for ϵ-amino groups was applied. Adlayers of Mefp-1 were exposed to an oxidant, either the enzyme, mushroom tyrosinase, or sodium periodate. Binding of alginate to adlayers was used to probe for accessibility of ϵ-amino groups. It was found that lysine residues lose the ability to bind alginate after exposure to sodium periodate, but that this loss is not clearly due to a reaction with L-dopa residues. There is a slight decrease of binding of alginate to adlayers of Mefp-1 exposed to either active or thermally deactivated mushroom tyrosinase, probably due to the obstruction of binding sites by bound enzyme. Adsorption kinetics of mushroom tyrosinase onto adlayers of Mefp-1 for active and thermally inactivated enzyme were nearly identical. Attenuated total reflection Fourier transform infrared spectroscopy was used to characterize these interactions at a germanium (Ge) interface.