ArticleACS applied materials & interfaces2025
Lignin-Based Mucus-Mimicking Antiviral Hydrogels with Enzyme Stability and Tunable Porosity.
Article in ACS applied materials & interfaces, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Upcycling Lignin into Porous Hybrid Beads and Sponges for Efficient Removal of Organic and Biological Contaminants from Water.ACS materials Au · 2026Article
- Protein-Linker Co-engineering for Broad-Spectrum Antiviral Development against Enveloped Viruses.ACS materials letters · 2026Article
- Hydrogels in Veterinary Vaccine Development: Types, Mechanisms, and Applications.Gels (Basel, Switzerland) · 2025Review
- Establishing a Xanthan Gum-Locust Bean Gum Mucus Mimic for Cystic Fibrosis Models: Yield Stress and Viscoelasticity Analysis.Biomimetics (Basel, Switzerland) · 2025Article
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Authors and funding
13 authors.
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Abstract
Mucus is a complex hydrogel that acts as a defensive and protective barrier in various parts of the human body. The rise in the level of viral infections has underscored the importance of advancing research into mucus-mimicking hydrogels for the efficient design of antiviral agents. Herein, we demonstrate the gram-scale synthesis of biocompatible, lignin-based virus-binding inhibitors that reduce waste and ensure long-term availability. The lignin-based inhibitors are equipped with sulfate moieties, which are known binding partners for many viruses, including SARS-CoV-2 and herpes viruses. In addition, cross-linking the synthesized inhibitors yielded hydrogels that mimicked native mucus concerning surface functionality and rheology. The degree of sulfation exhibits a very strong impact on the mesh size distribution of the hydrogels, which provides a new means to fine-tune the steric and electrostatic contributions of the virus-hydrogel interaction. This feature strongly impacts the sequestration capability of the lignin-based hydrogels, which is demonstrated by infection inhibition assays involving human herpes simplex virus 1, influenza A viruses, and the bacterium
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