September 27, 2011 - 11:22am
A communication by graduate student Conor Haney and coworkers from the Horne group was featured on the cover of a recent issue of ChemComm. In their paper, Haney, Loch and Horne report that oxime side-chain cross-links can promote alpha-helix formation by short peptides in aqueous solution. Covalent side-chain "stapling" is known to be a useful method to control peptide folding. The oxime staple examined by Haney et al. has the interesting properties of being both bio-orthogonal and dynamically reversible in water. Their findings suggest the potential to combine the known benefits of peptide stapling with template-assisted amplification to enable discovery of constrained polycyclic peptides that bind with high affinity to target proteins. Link to the cover: http://pubs.rsc.org/en/content/articlepdf/2011/cc/c1cc90142g Link to the article: http://dx.doi.org/10.1039/C1CC12010G