Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils
- Resource Type
- Authors
- Mireille Maria Anna Elisabeth Claessens; Marcel Karperien; Maurice C E van Dalen; Jonathan Vaneyck; Janine N. Post; Slav A. Semerdzhiev
- Source
- Langmuir
Langmuir, 37(24). American Chemical Society
- Subject
- Amyloid
UT-Hybrid-D
Biocompatible Materials
02 engineering and technology
010402 general chemistry
01 natural sciences
Viscoelasticity
Article
chemistry.chemical_compound
Adsorption
Tissue engineering
Electrochemistry
General Materials Science
Spectroscopy
Biomaterial
Hydrogels
Surfaces and Interfaces
021001 nanoscience & nanotechnology
Condensed Matter Physics
0104 chemical sciences
chemistry
Self-healing hydrogels
Biophysics
Muramidase
Lysozyme
0210 nano-technology
Protein adsorption
- Language
- ISSN
- 1520-5827
0743-7463
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.