Design flexibility
and modularity have emerged as powerful tools in the development of
functional self-assembled peptide nanostructures. In particular, the
tendency of peptides to form fibrils and nanotubes has motivated the
investigation of electron and, more recently, proton transport in
their fibrous films. In this study, we present a detailed characterization
by impedance spectroscopy of films of self-assembled cyclic octa-d,l-α-peptide self-assembled nanotubes with amine side
chains that promote proton transport. We show that the conductivity
of the peptide nanotube film, which is in the range of 0.3 mS cm–1, is within the same order of magnitude as that of
ultrathin films of Nafion, a benchmark proton conducting polymer.
In addition, we show that while slow diffusion processes at the interface
are present for both films, additional interface effects occur in
the peptide nanotube films at the same rate as their bulk proton transport
effects, further limiting charge transport at the interface. Overall,
our studies demonstrate the great potential of using peptides as building
blocks for the preparation of bioinspired supramolecular proton conducting
polymers with improved conductivity with respect to that of natural
systems.
The binding of peptide and proteins through multiple weak interactions is ubiquitous in nature. Biopanning has been used to “hijack” this multivalent binding for functionalization of surfaces. For practical applications...
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