« What Structures Have Turned on You? |
| Reversal of Type II Diabetes May Be Possible »
July 16, 2014
An Easy Way to Make Cyclic Peptides
If you ever find yourself needing to make large cyclic peptides, you now have a new option. This paper in Organic Letters describes a particularly clean way to do it: let glutathione-S-transferase (GST) do the work for you. Bradley Pentelute's group at MIT reports that if your protein has a glutathione attached at one end, and a pentafluoroaryl Cys at the other, that GST will step in and promote the nucleophilic aromatic substitution reaction to close the two ends together.
This is an application of their earlier work on the uncatalyzed reaction and on the use of GST for ligation.. Remarkably, the GST method seems to product very high yields of cyclic peptides up to at least 40 residues, and at reasonable concentration (10 mM) of the starting material, under aqueous conditions. Cyclic peptides themselves are interesting beasts, often showing unusual properties compared to the regular variety, and this method look as it will provide plenty more of them for study.
+ TrackBacks (0) | Category: Chemical Biology | Chemical News
POST A COMMENT
- RELATED ENTRIES
- XKCD on Protein Folding
- The 2014 Chemistry Nobel: Beating the Diffraction Limit
- German Pharma, Or What's Left of It
- Sunesis Fails with Vosaroxin
- A New Way to Estimate a Compound's Chances?
- Meinwald Honored
- Molecular Biology Turns Into Chemistry
- Speaking at Northeastern