at Peking University School of Pharmaceutical Sciences
the dong research group
Self-assembly Glycopeptides
Due to the good biocompatibility and controllable degradation, the self-assembly of glycopeptides has become a research hotspot in the fields of materials and biomedicine in recent years. By regulating the molecular structure of glycopeptides and changing the external environment, glycopeptide self-assembly with specific morphology and structure could be triggered by non-covalent bond forces such as hydrogen bonding, hydrophobic interaction and π-π stacking.
In our previous work, we found that peptide-β-glucan conjugates could self assemble into uniform nanoparticles that facilitate the delivery of antigens and binding to myeloid cells, thus leading to the activation of both innate and adaptive immunity. Based on this, we designed the self-assembling glycopeptide conjugates to generate a series of multivalently glycosylated nanoparticles, which may be able to interact with lectins that often targeted by complex natural carbohydrates. The immunostimulatory activities of these glyconanoparticles have been evaluated both in vitro and in vivo. And the results indicate that the mannose-modified NPs could act as an immune activator in both macrophage cell culture and mice vaccination.
More recently, we discovered that a dimeric tyrosine-rich glycopeptide could self-assemble to form hydrogels under the influence of glycans with varied stereochemistry. Based on mechanistic studies, a glycopeptide derived from unnatural D-amino acids and natural D-glucose has been designed and synthesized, and can afford a hydrogel with enzyme resistant properties.