Bioinspired peptide assemblies are promising candidates for use as proton-conducting materials in electrochemical devices and other advanced technologies. Progress toward applications requires establishing foundational structure-function relationships for transport in these materials. This experimental-theoretical study sheds light on how the molecular structure and proton conduction are linked in three synthetic cyclic peptide nanotube assemblies that comprise the three canonical basic amino acids (lysine, arginine, and histidine).
View Article and Find Full Text PDFDesign 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.
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