Long-Range Proton Transport in Films from a Reflectin-Derived Polypeptide
Chengyi Xu1, Nabin Kandel2, Xin Qiao2
1Department of Materials Science and Engineering, University of California, Irvine, Irvine, California 92697, United States.
ACS Applied Materials & Interfaces
|May 3, 2021
Summary
Researchers developed reflectin-derived polypeptide films that achieve long-range proton transport, a rare feat for bioelectronic materials. These films show conductivity and structural properties relevant for future bioinspired proton conductor development.
Area of Science:
- Biomaterials Science
- Bioelectronics
- Protein Engineering
Background:
- Protein and peptide-based materials are crucial for biological processes and bioelectronic devices.
- Demonstrating long-range proton transport in these materials remains a significant challenge.
Purpose of the Study:
- To fabricate and characterize films from a reflectin-derived polypeptide for proton conductivity.
- To investigate the relationship between the polypeptide's structure and its electrical functionality.
Main Methods:
- Fabrication of films from a reflectin-derived polypeptide.
- Electrical interrogation of device-integrated films.
- Physical characterization of the polypeptide films.
Main Results:
- Proton conductivities of approximately 0.4 mS/cm were achieved.
- Proton transport was sustained over distances of approximately 1 mm.
- The polypeptide exhibited characteristics analogous to the parent protein class.
Conclusions:
- The study demonstrates a novel bioinspired material for sustained, long-range proton transport.
- Findings provide insights into structure-function relationships for solid-state bio-proton conductors.
- The research contributes to the development of reflectin-based materials and other bioinspired proton conductors.
More Related Videos
Related Concept Videos
Protein Dynamics in Living Cells
2.4K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.4K
Protein Diffusion in the Membrane
5.0K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
5.0K
Protein Transport to the Thylakoids
2.5K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
2.5K
Protein Transport into the Inner Mitochondrial Membrane
4.3K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.3K
Energy to Drive Translocation
2.4K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.4K


