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- W2946935757 abstract "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." @default.
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- W2946935757 date "2019-05-30" @default.
- W2946935757 modified "2023-10-18" @default.
- W2946935757 title "Fish and Clips: A Convenient Strategy to Identify Tyrosinase Substrates with Rapid Activation Behavior for Materials Science Applications" @default.
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- W2946935757 doi "https://doi.org/10.1021/acsmacrolett.9b00244" @default.
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