Adsorption of chemically synthesized mussel adhesive peptide sequences containing DOPA on stainless steel |
| |
| Authors: | Neha Chandrasekaran Simone Dimartino Tejraj Janmale Steven P. Gieseg Conan J. Fee |
| |
| Affiliation: | 1. Department of Chemical and Process Engineering, University of Canterbury, Christchurch, New Zealand;2. Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand;3. Free Radical Biochemistry, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand;4. Department of Radiology, University of Otago Christchurch, New Zealand |
| |
| 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. |
| |
| Keywords: | adhesive peptides DOPA, stainless steel QCM‐D, mushroom tyrosinase |
|
|
