Journal
SMALL
Volume 18, Issue 11, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.202105456
Keywords
atomic force microscopy; elasticity; genetic engineering; material fatigue; mechanical strength; nanostructured protein materials; self-healing
Categories
Funding
- FPI fellowship from the Spanish Ministerio de Ciencia e Innovacion [BES-2016-077084]
- MICINN/FEDER EU (Spain) [RTI2018-096635-B-100]
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By genetically modifying proteins, researchers have successfully increased the fatigue resistance and self-healing capabilities of protein-based nanostructured materials, while maintaining high thermal stability. This provides a new approach for enhancing the performance of protein-based nanostructured materials.
Protein-based nanostructured materials are being developed for many biomedical and nanotechnological applications. Despite their many desirable features, protein materials are highly susceptible to disruption by mechanical stress and fatigue. This study is aimed to increase fatigue resistance and enhance self-healing of a natural protein-based supramolecular nanomaterial through permanent genetic modification. The authors envisage the conversion of a model nanosheet, formed by a regular array of noncovalently bound human immunodeficiency virus capsid protein molecules, into a supramolecular chain mail. Rationally engineered mutations allow the formation of a regular network of disulfide bridges in the protein lattice. This network links each molecule in the lattice to each adjacent molecule through one covalent bond, analogous to the rivetting of interlinked iron rings in the chain mail of a medieval knight. The engineered protein nanosheet shows greatly increased thermostability and resistance to mechanical stress and fatigue in particular, as well as enhanced self-healing, without undesirable stiffening compared to the original material. The results provide proof of concept for a genetic design to permanently increase fatigue resistance and enhance self-healing of protein-based nanostructured materials. They also provide insights into the molecular basis for fatigue of protein materials.
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