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Fish and Clips: A Convenient Strategy to Identify Tyrosinase Substrates with Rapid Activation Behavior for Materials Science Applications
journal contribution
posted on 2019-05-30, 12:34 authored by Justus Horsch, Patrick Wilke, Heike Stephanowitz, Eberhard Krause, Hans G. BörnerPeptides 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.
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OBOCenzyme-activated adhesivesdopaquinone residuesMaterials Science Applications Peptidessequences exhibit tyrosine residuestyrosine-bearing sequencesConvenient Strategyenzyme-activated coating behaviorpeptide libraryselection processsubstrate propertiesactivation kineticsIdentify Tyrosinase Substratestyrosinase oxidationRapid Activation BehaviorMALDI-TOF-MSsequence readout
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