Adsorption of chemically synthesized mussel adhesive peptide sequences containing DOPA on stainless steel. (8th April 2015)

• Record Type: Journal Article
• Authors: Chandrasekaran, Neha; Dimartino, Simone; Janmale, Tejraj; Gieseg, Steven P.; Fee, Conan J.
• Is Part Of: Journal of peptide science. Volume 21:Number 8(2015:Aug.)
• Page Start: 630
• Page End: 635
• Publication Date: 2015-04-08
• Subjects: Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2776
• Languages: English
• ISSNs: 1075-2617

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>L</italic>‐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 <italic>Mytilus edulis</italic> 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 <italic>M. edulis</italic> foot protein 5 motifs. Copyright © 2015 European Peptide Society and John Wiley &amp; Sons, Ltd.</p> </abstract>