Adsorption of chemically synthesized mussel adhesive peptide sequences containing DOPA on stainless steel.

Neha Chandrasekaran, Simone Dimartino, Tejraj Janmale, Steven P Gieseg, Conan J Fee

Index: J. Pept. Sci. 21 , 630-5, (2015)

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Abstract

The adsorption of proteins at solid-liquid interfaces is important in biosensor and biomaterial applications. Marine mussels affix themselves to surfaces using a highly cross-linked, protein-based adhesive containing a high proportion of L-3,4-dihydroxyphenylalanine (DOPA) residues. In this work, the effect of DOPA residues on protein adhesion on stainless steel surfaces was studied using a quartz crystal microbalance with dissipation system. The adsorption of two repetitive peptide motifs, KGYKYYGGSS and KGYKYY, from the mussel Mytilus edulis foot protein 5 on stainless steel was studied before and after chemo-enzymatic modification of tyrosine residues to DOPA using mushroom tyrosinase. Conversion from tyrosine to DOPA, evaluated by HPLC, was in the range 70-99%. DOPA-modified sequences showed fourfold greater adhesion than unmodified M. edulis foot protein 5 motifs.Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.