Expression of a model peptide of a marine mussel adhesive protein in Escherichia coli and characterization of its structural and functional properties

An expression system for a chemically synthesized gene, encoding a model peptide of marine mussel adhesive protein, was constructed in Escherichia coli under regulation of the T7-promoter. The model peptide consisted of six repeats of the decapeptide AKPSYPPTYK. Although the product was expressed as an inclusion body, we were able to solubilize it successfully, using acetic acid. The higher-order structure of this model peptide was investigated using CD spectroscopy and NMR spectroscopy. Using the modified enzyme, mushroom tyrosinase, the tyrosine residue was hydroxylated to 3,4-dihydoxyphenylalanine (Dopa), and the resulting modified peptide was polymerized, solidified, and insolubilized spontaneously.