Rheology of reconstituted silk fibroin protein gels: the epitome of extreme mechanics.
basic_science · Level V
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- Record sourced from PubMed, PMID 25489795.
- Also identified by DOI 10.1039/c4sm02079k.
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Abstract
In nature, silk fibroin proteins assemble into hierarchical structures with dramatic mechanical properties. With the hope of creating new classes of on demand silk-based biomaterials, Bombyx mori silk is reconstituted back into stable aqueous solutions that can be reassembled into functionalized materials; one strategy for reassembly is electrogelation. Electrogels (e-gels) are particularly versatile and can be produced using electrolysis with small DC electric fields. We characterize the linear and nonlinear rheological behavior of e-gels to provide fundamental insights into these distinct protein-based materials. We observe that e-gels form robust biopolymer networks that exhibit distinctive strain hardening and are recoverable from strains as large as γ=27, i.e. 2700%. We propose a simple microscopic model that is consistent with local restructuring of single proteins within the e-gel network.
Medical subject headings
- Fibroins
- Mechanical Phenomena
- Rheology