A peroxidase-sensitive desthiobiotin-phenol (DBP) probe th at offers more efficient recovery of DBP-labeled peptides from streptavidin beads and stronger mass spectrometry intensity of modified membrane proteins and achieves greater sensitivity for tyrosine residues detection. DBP shows a similar reactivity to the protein when it is converted to the phenoxyl radical state as biotin-phenol/biotin-tyramide (BP) in ascorbate peroxidase (APEX) proximity labeling. DBP exhibits reduced affinity to streptavidin and does not suffer from sulfur oxidation issue during the radical generation.
