Abstract
Transition metal-mediated arylation chemistry is emerging as a powerful tool for the selective modification of native peptides and proteins, providing new opportunities in the field of bioconjugation. This highlight paper will summarize recent methodologies for the regio- and chemoselective arylation of select proteinogenic side chains and backbone amide N-H bonds within unprotected peptides and proteins. The importance of the metal-ligand complex in achieving tunable selectivity and the inherent benefits of arylation as a mode of covalent protein modification will be highlighted.
| Original language | English |
|---|---|
| Pages (from-to) | 1360-1364 |
| Number of pages | 5 |
| Journal | Australian Journal of Chemistry |
| Volume | 69 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2016 |
| Externally published | Yes |
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