a distinction between different materials like for instance between highly related semiconductor surfaces or between different noble metals. [9,10] Peptides that discriminate glass from poly(siloxane)s or printed from nonprinted regions of office laser printer printouts, make selective coatings for low-cost production of functional patterns available. [11,12] Recently, phage display screening was extended to select tyrosinase activatable peptides that were tailored to bind to Al 2 O 3 and show a distinct property transition from weak to strong/irreversible binders after enzymatic processing. [13] Adhesive properties of poly(ethylene glycol)-peptide (PEG-peptide) conjugates from those sequences were rapidly activated by tyrosinase, enabling adhesion to Al 2 O 3 under seawater model conditions. This led to the formation of antifouling coatings that resisted intense washing steps with seawater equivalents and suppressed nonreversible full blood serum adsorption. [14] The implemented tyrosinase activation that oxidizes tyrosine residues within the sequences to 3,4-dihydroxy-l-phenylalanine (Dopa) residues has analogies to processes found in the adhesive apparatus of marine mussels, where the presence of Dopa is essential to constitute adhesion and cohesion. [15] The relevance of Dopa residues for adhesion is commonly accepted. While this forms the base for a rich class of musselglue inspired polymers, [16] the contribution of the sequence environment of Dopa residues is frequently underestimated. Studies on mussel foot proteins suggest profound contributions of Dopa-associated sequences, not only modulating the binding strengths of Dopa residues but also realizing adaptiveness to various surfaces. [17,18] Hence, understanding the underlying structural basis for the interaction of synthetic mussel-inspired peptides with, e.g., Al 2 O 3 surfaces might open opportunities to improve artificial adhesives. For that purpose, high-resolution solution-state NMR is a powerful tool, allowing for protein structure determination and functional analysis. [19] Protein interactions can be revealed on a molecular level by nuclear Overhauser enhancement (NOE) based transient, exchange (NOESY/EXSY) [20,21] and saturation transfer difference (STD) [22] NMR spectroscopy. Recently, Mirau et al. applied these methods to gain insight into peptide-nanoparticle 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 (HSY*SGWSPY*RSG (Y* = l-Dopa)) that was previously selected by phage-display to adhere to Al 2 O 3 after enzymatic activation. Molecular level insights into the full-length adhesion domain at Al 2 O 3 surfaces are provided by a divergent-convergent analysis, combining nuclear Overhauser enhancement based 2D NOESY and saturation transfer difference NMR analysis of submotifs along with molecular dynamics simulations of the full-length peptide. The peptide is divided into two submotifs, each con...