News

Full Abstract: Mussel glue-proteins undergo structural transitions at material interfaces to optimize adhesive surface contacts. Those intriguing structure responses are mimicked by a mussel-glue mimetic peptide (HS Y*SGWSPY*RSG (Y* = L-Dopa)) that was previously selected by phage-display to adhere to Al2O3 after enzymatic-activation. Molecular level insights into the full-length adhesion domain at Al2O3 surfaces are provided by a divergent-convergent analysis, combining nuclear Overhauser enhancement based 2D NOESY and saturation transfer difference NMR analysis of sub-motifs along with molecular dynamics simulations of the full-length peptide. The peptide is divided into two sub motifs, each containing one Dopa “anchor” (either Motif-1 or Motif-2). The analysis proves Motif-1 to constitute a dynamic Al2O3 binder and adopting an “M”-structure with multiple surface contacts. Motif-2 binds stronger by two surface contacts, forming a compact “C”-structure. Using these datasets as constraints enables to predict the structure and propose a binding process model of the full-length peptide adhering to Al2O3 surface.