2019
DOI: 10.1098/rsif.2018.0775
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Interfibril hydrogen bonding improves the strain-rate response of natural armour

Abstract: Fish scales are laminated composites that consist of plies of unidirectional collagen fibrils with twisted-plywood stacking arrangement. Owing to their composition, the toughness of scales is dependent on the intermolecular bonding within and between the collagen fibrils. Adjusting the extent of this bonding with an appropriate stimulus has implications for the design of next-generation bioinspired flexible armours. In this investigation, scales were exposed to environments of water or a polar solvent … Show more

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Cited by 11 publications
(8 citation statements)
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References 67 publications
(94 reference statements)
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“…As previously highlighted, the relative contributions of interfibrillar sliding and fibril rotation may depend on the free length of the fibers (i.e., the width of the specimens) and that was not considered in the present investigation. Another limitation is that the scale properties were evaluated at a single strain rate and the relative contribution of interpeptide bonds is a function of strain rate [2] . Future studies could address the changes in contributing mechanisms as a function of strain rate.…”
Section: Discussionmentioning
confidence: 99%
“…As previously highlighted, the relative contributions of interfibrillar sliding and fibril rotation may depend on the free length of the fibers (i.e., the width of the specimens) and that was not considered in the present investigation. Another limitation is that the scale properties were evaluated at a single strain rate and the relative contribution of interpeptide bonds is a function of strain rate [2] . Future studies could address the changes in contributing mechanisms as a function of strain rate.…”
Section: Discussionmentioning
confidence: 99%
“…After biomodification, an increase in the damping capacity was identified at the microscale level and could indicate that modified dentin displays a higher capacity to dissipate energy during mechanical vibration than unmodified dentin matrix. 57,58 Interfibrillar bonds formed by Trimer-C and Trimer-EC may enable an increase in fibrillar sliding and the conformational flexibility of PAC-protein complexes that, combined with fluid motions throughout interfibrillar spaces of the ECM, induce a more viscous-like behavior of dentin. Conversely, the reduction of the damping capacity observed at the nanoscale could be due to the increase in intermolecular and interfibrillar cross-linking and possible occupation of gap and overlap zones by these bonds.…”
Section: Biochemical Characterization Of the Dentin Matrixmentioning
confidence: 99%
“…Mechanical properties such as elastic modulus, ultimate tensile strength, strain at failure, modulus of toughness and stiffness were also evaluated by uniaxial tensile testing and transverse puncture testing on C. carpio scales [61]. Here, scales were obtained from near the head, middle and tail region of multiple fish, and then evaluated after being fully hydrated in water or after exposure to a polar solvent (ethanol) to find the effect of the polar solvent on the mechanical properties of the scales.…”
Section: Mechanical Characterization Of Natural Fish Scalesmentioning
confidence: 99%