Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient “click” ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme). The site-...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
Wiley Blackwell
2015
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| Online Access: | http://hdl.handle.net/1721.1/95629 https://orcid.org/0000-0001-9519-7456 https://orcid.org/0000-0003-1632-5195 |
| Summary: | Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient “click” ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme). The site-specific modification of one cysteine residue was possible in the presence of other unprotected cysteine residues and reactive functional groups. |
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