Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels DOI Creative Commons
Jonas Proksch, Marlene C. S. Dal Colle, Frederick Heinz

и другие.

Опубликована: Янв. 23, 2024

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

Язык: Английский

Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels DOI Creative Commons
Jonas Proksch, Marlene C. S. Dal Colle, Frederick Heinz

и другие.

Опубликована: Янв. 23, 2024

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

Язык: Английский

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