What is it about?
A new strategy is demonstrated for making peptides helical, using a carbohydrate to bridge between sidechains at each end of a pentapeptide. CD and NMR spectra establish that both an a-helix and a 310-helix structure can form depending upon the bridge. Strategies that have been developed to make macrocyclic peptides helical, include cross-linking amino acids through their side chains or head/tail to side chain, or incorporating a hydrogen-bond surrogate. Such approaches have limitations, increasing synthetic complexity, reducing solubility, and inducing cell lysis due to membrane damage.In this study we investigate the potential to use glucuronic acid as a linking motif, which can provide different linker sites and also alter peptide solubility.
Featured Image
Why is it important?
It is a big challenge to make peptide permeable. Most efforts have been devoted to promoting peptide with passive permeability by making peptide more hydrophobic. However, not much efforts were paid on using hydrophilic linkers or confer peptide with hydrophilicity to increase active transportation. We try to study the peptide structure and functions change after glycosylation.
Perspectives
It should be noted, the certain structure of peptide has unique functions. In the future, we want to demonstrate the glycosylation can not only induce peptide to helical, but also can be applied to modify some potential peptide leads, to make peptide more druggable, with better permeability, solubility, stability, even oral bioavailability.
Chongyang Wu
University of Queensland
Read the Original
This page is a summary of: Glucuronic acid as a helix-inducing linker in short peptides, Chemical Communications, January 2018, Royal Society of Chemistry,
DOI: 10.1039/c7cc09785a.
You can read the full text:
Resources
Contributors
The following have contributed to this page
