Horsch, Justus Wilke, Patrick Stephanowitz, Heike Krause, Eberhard Bòˆrner, Hans G. Fish and Clips: A Convenient Strategy to Identify Tyrosinase Substrates with Rapid Activation Behavior for Materials Science Applications Peptides with suitable substrate properties for a specific tyrosinase are selected by combinatorial means from a one-bead-one-compound (OBOC) peptide library. The identified sequences exhibit tyrosine residues that are rapidly oxidized to 3,4-dihydroxyphenylalanine (Dopa), making the peptides interesting for enzyme-activated adhesives. The selection process of peptides involves tyrosinase oxidation of tyrosine-bearing sequences on a solid support, yielding dopaquinone residues (fish from the sequence pool), to which thiol-functional fluorescent probes attach by Michael-reaction (clip to mark). Labeled supports are isolated and sequence readout is feasible by MALDI-TOF-MS/MS to reveal peptides, while activation kinetics as well as enzyme-activated coating behavior are verifying the proper selection. OBOC;enzyme-activated adhesives;dopaquinone residues;Materials Science Applications Peptides;sequences exhibit tyrosine residues;tyrosine-bearing sequences;Convenient Strategy;enzyme-activated coating behavior;peptide library;selection process;substrate properties;activation kinetics;Identify Tyrosinase Substrates;tyrosinase oxidation;Rapid Activation Behavior;MALDI-TOF-MS;sequence readout 2019-05-30
    https://acs.figshare.com/articles/journal_contribution/Fish_and_Clips_A_Convenient_Strategy_to_Identify_Tyrosinase_Substrates_with_Rapid_Activation_Behavior_for_Materials_Science_Applications/8204153
10.1021/acsmacrolett.9b00244.s001