Many marine organisms are able to synthesize strong adhesive materials for affixing themselves to almost any surface.  Mussels (Mytilus edulis), for example, make a wet setting, cross-linked, protein-based glue for sticking to rocks and each other.  Characterization of mussel plaques and precursor proteins has revealed large amounts of 3,4-dihyroxyphenylalanine (DOPA) at levels up to 22% of the total amino acid content.  Generation of mussel adhesive plaques is dependent on the cross-linking of DOPA proteins, with some DOPA proteins contacting the surface while others form an outer, protective coating.  Peptide mimics are being studied to obtain atom-by-atom level insights on the chemical cross-links giving rise to the performance of this intriguing biological material.  Characterization efforts to date indicate that iron(III) provides the key cross-linker for this process.  Additionally, since mussel proteins cannot be extracted in practical quantities, commercially available proteins, such as bovine serum albumin (BSA) are more appealing for bulk materials.  Therefore, we are incorporating mussel adhesive chemistry into non-adhesive proteins.  Using a tyrosinase enzyme, we are oxidizing tyrosines to DOPAs.  The bulk adhesive properties of these new products are being examined.

Characterization and replication of DOPA adhesion in peptides and proteins

246th National Meeting (2013)

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