A new linker has been developed by using a simple carbohydrate to stabilize helical structure.
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.
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.
The following have contributed to this page: Chongyang Wu
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