Light-Modulated Cationic and Anionic Transport across Protein Biopolymers*.

Light is a convenient source of energy and the heart of light-harvesting natural systems and devices. Here, we show light-modulation of both the chemical nature and ionic charge carrier concentration within a protein-based biopolymer that was covalently functionalized with photoacids or photobases. We explore the capability of the biopolymer-tethered photoacids and photobases to undergo excited-state proton transfer and capture, respectively. Electrical measurements show that both the photoacid- and photobase-functionalized biopolymers exhibit an impressive light-modulated increase in ionic conductivity. Whereas cationic protons are the charge carriers for the photoacid-functionalized biopolymer, water-derived anionic hydroxides are the suggested charge carriers for the photobase-functionalized biopolymer. Our work introduces a versatile toolbox to photomodulate both protons and hydroxides as charge carriers in polymers, which can be of interest for a variety of applications.

A Protein-Based Free-Standing Proton-Conducting Transparent Elastomer for Large-Scale Sensing Applications.

A most important endeavor in modern materials' research is the current shift toward green environmental and sustainable materials. Natural resources are one of the attractive building blocks for making environmentally friendly materials. In most cases, however, the performance of nature-derived materials is inferior to the performance of carefully designed synthetic materials. This is especially true for conductive polymers, which is the topic here. Inspired by the natural role of proteins in mediating protons, their utilization in the creation of a free-standing transparent polymer with a highly elastic nature and proton conductivity comparable to that of synthetic polymers, is demonstrated. Importantly, the polymerization process relies on natural protein crosslinkers and is spontaneous and energy-efficient. The protein used, bovine serum albumin, is one of the most affordable proteins, resulting in the ability to create large-scale materials at a low cost. Due to the inherent biodegradability and biocompatibility of the elastomer, it is promising for biomedical applications. Here, its immediate utilization as a solid-state interface for sensing of electrophysiological signals, is shown.

The porphyrin ring rather than the metal ion dictates long-range electron transport across proteins suggesting coherence-assisted mechanism.

The fundamental biological process of electron transfer (ET) takes place across proteins with common ET pathways of several nanometers. Recent discoveries push this limit and show long-range extracellular ET over several micrometers. Here, we aim in deciphering how protein-bound intramolecular cofactors can facilitate such long-range ET. In contrast to natural systems, our protein-based platform enables us to modulate important factors associated with ET in a facile manner, such as the type of the cofactor and its quantity within the protein. We choose here the biologically relevant protoporphyrin molecule as the electron mediator. Unlike natural systems having only Fe-containing protoporphyrins, i.e., heme, as electron mediators, we use here porphyrins with different metal centers, or lacking a metal center. We show that the metal redox center has no role in ET and that ET is mediated solely by the conjugated backbone of the molecule. We further discuss several ET mechanisms, accounting to our observations with possible contribution of coherent processes. Our findings contribute to our understanding of the participation of heme molecules in long-range biological ET.

Enhanced Proton Conductivity across Protein Biopolymers Mediated by Doped Carbon Nanoparticles.

Carbon nanoparticles, known as carbon-dots (C-Dots), are famous for their optoelectronic properties. Here it is shown that C-Dots can also mediate protons, where protein biopolymers are used as the protonic transport matrix. Energy transfer measurements indicate that different doped C-Dots bind to the protein biopolymer in different efficiencies. Electrical impedance measurements reveal enhanced conductance across the protein biopolymer upon C-Dots integration, dependent on the doping type. The enhanced conductivity is attributed to protonic conduction due to the large observed kinetic isotope effect, resulting in one of the highest measured proton conductivity across protein biopolymers. Transistor measurements show that the various doped C-Dots-protein biopolymer exhibit different increase in charge carrier density and in carrier mobility, suggesting different modes of proton transport. The ability of C-Dots to support protonic conduction opens a field of carbon-based protonic nanoparticles and due to the formation simplicity of C-Dots they can be integrated in a variety of protonic devices.

Correction: Exploring long-range proton conduction, the conduction mechanism and inner hydration state of protein biopolymers.

[This corrects the article DOI: 10.1039/C9SC04392F.].

Exploring long-range proton conduction, the conduction mechanism and inner hydration state of protein biopolymers.

Proteins are the main proton mediators in various biological proton circuits. Using proteins for the formation of long-range proton conductors is offering a bioinspired approach for proton conductive polymers. One of the main challenges in the field of proton conductors is to explore the local environment within the polymers, along with deciphering the conduction mechanism. Here, we show that the protonic conductivity across a protein-based biopolymer can be hindered using straightforward chemical modifications, targeting carboxylate- or amine-terminated residues of the protein, as well as exploring the effect of surface hydrophobicity on proton conduction. We further use the natural tryptophan residue as a local fluorescent probe for the inner local hydration state of the protein surface and its tendency to form hydrogen bonds with nearby water molecules, along with the dynamicity of the process. Our electrical and spectroscopic measurements of the different chemically-modified protein materials as well as the material at different water-aprotic solvent mixtures result in our fundamental understanding of the proton mediators within the material and gaining important insights on the proton conduction mechanism. Our biopolymer can be used as an attractive platform for the study of bio-related protonic circuits as well as a proton conducting biopolymer for various applications, such as protonic transistors, ionic transducers and fuel cells.