AI Article Synopsis
- * Mussel foot protein 5, with specific peptide motifs, was tested on stainless steel before and after converting tyrosine to DOPA using mushroom tyrosinase.
- * Results showed that DOPA-modified peptides adhered four times better to stainless steel compared to the unmodified versions, indicating the significance of DOPA in enhancing protein adhesion.
Article 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.
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| http://dx.doi.org/10.1002/psc.2776 | DOI Listing |
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