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Self-assembly of collagen bundles and enhanced piezoelectricity induced by chemical crosslinking.

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Kar-Narayan, Sohini  ORCID logo
Best, Serena M 
Cameron, Ruth E 


The piezoelectricity of collagen is purported to be linked to many biological processes including bone formation and wound healing. Although the piezoelectricity of tissue-derived collagen has been documented across the length scales, little work has been undertaken to characterise the local electromechanical properties of processed collagen, which is used as a base for tissue-engineering implants. In this work, three chemically distinct treatments used to form structurally and mechanically stable scaffolds-EDC-NHS, genipin and tissue transglutaminase-are investigated for their effect on collagen piezolectricity. Crosslinking with EDC-NHS is noted to produce a distinct self-assembly of the fibres into bundles roughly 300 nm in width regardless of the collagen origin. These fibre bundles also show a localised piezoelectric response, with enhanced vertical piezoelectricity of collagen. Such topographical features are not observed with the other two chemical treatments, although the shear piezoelectric response is significantly enhanced upon crosslinking. These observations are reconciled by a proposed effect of the crosslinking mechanisms on the molecular and nanostructure of collagen. These results highlight the ability to modify the electromechanical properties of collagen using chemical crosslinking methods.



Collagen, Cross-Linking Reagents, Elastic Modulus, GTP-Binding Proteins, Iridoids, Microscopy, Atomic Force, Nanostructures, Protein Glutamine gamma Glutamyltransferase 2, Succinimides, Tissue Engineering, Transglutaminases

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Royal Society of Chemistry (RSC)
Engineering and Physical Sciences Research Council (EP/N019938/1)
European Research Council (639526)
ERC, Bill and Melinda Gates Foundation, Geistlich Pharma AG
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