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: | Zhang, Chi, Spokoyny, Alexander M., Zou, Yekui, Pentelute, Bradley L., Simon, Mark |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Chemistry |
Format: | Article |
Language: | en_US |
Published: |
Wiley Blackwell
2015
|
Online Access: | http://hdl.handle.net/1721.1/95629 https://orcid.org/0000-0001-9519-7456 https://orcid.org/0000-0003-1632-5195 |
Similar Items
-
Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides
by: Zou, Yekui, et al.
Published: (2015) -
A Perfluoroaryl-Cysteine S[subscript N]Ar Chemistry Approach to Unprotected Peptide Stapling
by: Spokoyny, Alexander M., et al.
Published: (2015) -
Organometallic palladium reagents for cysteine bioconjugation
by: Vinogradova, Ekaterina V., et al.
Published: (2017) -
Purification of glutathione S-transferase (GST) using mixed mode chromatography
by: M., Sivapragasam, et al.
Published: (2014) -
Insecticide toxicity, glutathione transferases and carboxylesterase activities in the larva of the Aedes mosquito
by: Shamaan, N.A., et al.
Published: (1993)