Generation of electric potential upon external stimulus has attracted much attention for the development of highly functional sensors and devices. Herein, we report large-displacement, fast actuation in the self-assembled engineered repeat protein Consensus Tetratricopeptide Repeat protein (CTPR18) materials. The ionic nature of the CTPR18 protein coupled to the long-range alignment upon self-assembly results in the measured conductivity of 7.1 × 10 S cm, one of the highest reported for protein materials. The change of through-thickness morphological gradient in the self-assembled materials provides the means to select between faster, highly water-sensitive actuation or vastly increased mechanical strength. Tuning of the mode of motion, e.g., bending, twisting, and folding, is achieved by changing the morphological director. We further show that the highly ionic character of CTPR18 gives rise to piezo-like behavior in these materials, exemplified by low-voltage, ionically driven actuation and mechanically driven generation/discharge of voltage. This work contributes to our understanding of the emergence of stimuli-responsiveness in biopolymer assemblies.
Complex hierarchical structures provide beneficial structure-property relationships that can be exploited for a variety of applications in engineering and biomedical fields. Here we report on molecular organization and resulting mechanical properties of self-assembled designed repeat-protein films. Wide-angle X-ray diffraction indicates the designed 18-repeat concensus tetratricopeptide repeat protein (CTPR18) orients normal to the casting surface, while small-angle measurements and electron microscopy show a through-plane transversely aligned laminar sheet-like morphology. Self-assembly is driven by the combination of CTPRs head-to-tail stacking and weak dipole-dipole interactions. We highlight the effect that this hierarchical structure has on the material's mechanical properties. We use nanoindentation and dynamic mechanical analysis to test the mechanical properties over multiple length scales, from the molecular level to the bulk. We find that morphology predictably affects the film's mechanics from the nano- to the macroscale, with the axial modulus values ranging from 2 to 5 GPa. The predictable nature of the structure-property relationship of CTPR proteins and their assemblies proves them a promising platform for material engineering.
In the past two decades researchers have shown great interest in mimicking biological structures and their complex structure–property relationships. Herein we highlight examples of hydrogels and bioelectronic materials that illustrate the rational design of material properties and function.
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