ArticleLangmuir : the ACS journal of surfaces and colloids2021
Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils.
Article in Langmuir : the ACS journal of surfaces and colloids, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Enabling water-based high-density nanoparticles assembly by using silk fibroin as an adsorbate.Nature communications · 2026Article
- Choice of Protein, Not Its Amyloid-Fold, Determines the Success of Amyloid-Based Scaffolds for Cartilage Tissue Regeneration.ACS omega · 2023Article
- Multidomain peptide hydrogel adjuvants elicit strong bias towards humoral immunity.Biomaterials science · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical applications the gels have to function in compositionally complex physiological solutions, their rheological behavior is typically only characterized in simple buffers. Here we show that the viscoelastic response of networks of amyloid fibrils of the protein lysozyme in biologically relevant solutions substantially differs from the response in simple buffers. We observe enhanced energy dissipation in both cell culture medium and synovial fluid. We attribute this energy dissipation to interactions of the amyloid fibrils with other molecules in these solutions and especially to the adsorption of the abundantly present protein serum albumin. This finding provides the basis for a better understanding of the performance of amyloid hydrogels in biomedical applications.
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Registered trials
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