12 research outputs found
Protein Self-Assemblies That Can Generate, Hold, and Discharge Electric Potential in Response to Changes in Relative Humidity
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<sup>–2</sup> S
cm<sup>–1</sup>, 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
Protein Self-Assemblies That Can Generate, Hold, and Discharge Electric Potential in Response to Changes in Relative Humidity
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<sup>–2</sup> S
cm<sup>–1</sup>, 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
Protein Self-Assemblies That Can Generate, Hold, and Discharge Electric Potential in Response to Changes in Relative Humidity
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<sup>–2</sup> S
cm<sup>–1</sup>, 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
Protein Self-Assemblies That Can Generate, Hold, and Discharge Electric Potential in Response to Changes in Relative Humidity
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<sup>–2</sup> S
cm<sup>–1</sup>, 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
Bioinorganic Interface: Mechanistic Studies of Protein-Directed Nanomaterial Synthesis
Proteins
and peptides have attracted much attention as templates
for one-pot synthesis of biocompatible gold nanoparticles. While numerous
natural and <i>de novo</i> protein sequences have been used,
the actual mechanism of nanoparticle nucleation and growth from the
protein matrix is not well understood. In this study we utilized engineered
consensus tetratricopeptide repeat protein (CTPR) to probe the bioinorganic
interface during gold nanoparticle synthesis. The binding of CTPR
to gold ions and the gold nanoparticle surface was investigated using
fluorescence spectroscopy and heteronuclear single quantum coherence
NMR spectroscopy to provide residue-specific measurements. This work
provides a foundation for the rational design of proteins for synthesis
of tailored functional nanomaterials for biological, medical, and
optical applications