Selective metal-site-guided arylation of proteins
We describe a palladium-mediated S-arylation method that exploits natural metal-binding motifs to ensure high site-selectivity for a proximal reactive residue. This allows the chemical identification not only of proteins that bind metals but the environment of the metal binding site itself through p...
| Main Authors: | , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
American Chemical Society
2016
|
| Summary: | We describe a palladium-mediated S-arylation method that exploits natural metal-binding motifs to ensure high site-selectivity for a proximal reactive residue. This allows the chemical identification not only of proteins that bind metals but the environment of the metal binding site itself through proteomic analysis of arylation sites. The transformation is easy to perform under standard conditions, does not require the isolation of a reactive Ar-Pd complex, is broad in scope and is applicable in cell lysates as well as to covalent inhibition/modulation of metal-dependent enzymatic activity. |
|---|