Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels

23 January 2024, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Mucus is a complex biological hydrogel that acts as a barrier for almost everything entering or exiting the body. It is therefore of emerging interest for biomedical and pharmaceutical applications. Besides water, the most abundant components are the large and densely glycosylated mucins, a family of glycoproteins with sizes of up to 20 MDa and a carbohydrate content of up to 80 wt%. Here, we designed and explored a library of glycosylated peptides to deconstruct the complexity of mucus. By using the well characterised hFF03 coiled-coil system as a hydrogel-forming peptide scaffold, we systematically probed the contribution of single glycans to the secondary structure as well as the formation and the viscoelastic properties of the resulting hydrogels. We show that glycan-decoration does not affect α helix and coiled-coil formation while it alters gel stiffness. By using oscillatory macrorheology, dynamic light scattering microrheology and fluorescence lifetime-based nanorheology, we characterised the glycopeptide materials over several length scales. Molecular simulations revealed that the glycosylated linker may extend into the solvent, but more frequently interacts with the peptide, thereby likely modifying the stability of the self-assembled peptide fibres. The results of this systematic study highlight the interplay between glycan structure and hydrogel properties and may guide the development of synthetic mucus mimetics.


glycopeptide library
peptide self-assembly
peptide hydrogels

Supplementary materials

Supporting Information - Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels
General methods, synthetic and analytical details


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