Influence of sodium periodate and tyrosinase on binding of alginate to adlayers of mytilus edulis foot protein 1
Suci, Peter A.
Geesey, Gill G.
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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.
Suci, P.A. and G.G. Geesey, "Influence of Sodium Periodate and Tyrosinase on Binding of Alginate to Adlayers of Mytilus edulis Foot Protein 1,"" Journal of Colloid and Interface Science, 230:3 (2000).