A catch-and-release approach to selective modification of accessible tyrosine residues

Christopher Allan, Miroslav Kosar, Christina V Burr, Colin Logan Mackay, Rory R Duncan, Alison Nicola Hulme

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The tyrosine side chain is amphiphilic leading to significant variations in the surface exposure of tyrosine residues in the folded structure of a native sequence protein. This variability can be exploited to give residue-selective functionalization of a protein substrate by using a highly reactive diazonium group tethered to an agarose-based resin. This novel catch-and-release approach to protein modification has been demonstrated for proteins with accessible tyrosine residues, which are compared with a control group of proteins in which there are no accessible tyrosine residues. MS analysis of the modified proteins showed that functionalization was highly selective, but reactivity was further attenuated by the electrostatic environment of any individual residue. Automated screening of PDB structures allows identification of potential candidates for selective modification by comparison with the accessibility of the tyrosine residue in a benchmark peptide (GYG).
Original languageEnglish
Early online date13 Sept 2018
Publication statusE-pub ahead of print - 13 Sept 2018


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