Abstract
Biomolecular proton conducting materials have been touted as promising for seamlessly and directly interfacing natural biological systems with traditional artificial electronics. As such, proton conduction has been explored for a variety of protein- and polypeptide-based materials. Within this context, cephalopod structural proteins called reflectins have demonstrated several favorable properties, including outstanding electrical figures of merit as proton conductors and intrinsic biocompatibility with cellular systems. However, the processing of reflectins into films has typically used low-throughput material-intensive strategies and has often required organic solvents. Herein, we report the preparation of devices from active layers fabricated via inkjet printing of reflectin solubilized in water and the systematic evaluation of their electrical performance. Taken together, our findings represent a step forward in the manufacturing and development of unconventional bioelectronic platforms from the reflectin family of proteins.
Highlights
Proton conduction has been explored in a number of different protein- and polypeptide-based architectures, such as films from the cephalopod protein reflectin,8 mats from bovine serum albumin (BSA),9 membranes from squid ring teeth proteins,10 fibers from amyloid-β peptides,11 and composites from MnOx/tyrosinerich peptides
We first expressed, characterized, and solubilized both the wild type Doryteuthis (Loligo) pealeii reflectin A1 (WT RfA1) protein and a variant of this protein with an additional six histidine residues incorporated at its N-terminus
We in turn characterized both types of printed films with optical microscopy, finding raised edges around the perimeter presumably due to solvent evaporation, as well as with atomic force microscopy (AFM), finding thicknesses of
Summary
Biomolecular proton conducting materials have been touted as promising for seamlessly and directly interfacing natural biological systems with traditional artificial electronics.1–7 Within this context, protein-based proton conductors feature several advantages, including well-defined sequences, modular structural characteristics, controllable self-assembly properties, ease of production, customizable physical properties, and intrinsic biocompatibility.4–16 proton conduction has been explored in a number of different protein- and polypeptide-based architectures, such as films from the cephalopod protein reflectin,8 mats from bovine serum albumin (BSA),9 membranes from squid ring teeth proteins,10 fibers from amyloid-β peptides,11 and composites from MnOx/tyrosinerich peptides.12 Among these materials, different reflectin isoforms have distinguished themselves as efficacious naturally occurring proton conductors with relatively high bulk conductivities of ∼3 × 10−3 S cm−1 and carrier mobilities of ∼0.01 cm2 V−1 s−1,8,13 enabling applications as diverse as protonic transistors,14 photochemically dopable devices,15 and protochromic color-changing platforms.16the inherent biocompatibility of reflectins has been exemplified by their ability to support the growth and differentiation of human and murine neural stem and progenitor cells17,18 and by their utility for the optical engineering of human cells.19reflectins’ technological potential has been hampered by typically low-throughput material-intensive processing strategies, such as drop-casting [as shown in Fig. 1(a)], and by the frequent need for organic solvents, such as hexafluoroisopropanol (HFIP).20–26 there exists an impetus for the development and validation of new approaches to the fabrication of reflectin-based films and structures for electrical device and other applications.
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