Proton‐Conductive Melanin‐Like Fibers through Enzymatic Oxidation of a Self‐Assembling Peptide

• DOI: 10.1002/adma.202003511
• Publication Date: 2020-10-15T18:35:37Z
• Authors: Samala Murali Moh...; Eileen Raßlenberg; Sian Sloan‐Dennison; Travis Hesketh; Ohad Silberbush; Tell Tuttle; Ewen Smith; Duncan Graham; Karen Faulds; Rein V. Ulijn; Nurit Ashkenasy; Ayala Lampel
• Keywords: Tripeptide; Morphology

Abstract Melanin pigments have various properties that are of technological interest including photo‐ and radiation protection, rich coloration, electronic functions. Nevertheless, laboratory‐based synthesis melanin melanin‐like materials with morphologies chemical structures specifically optimized for these applications, is currently not possible. Here, produced by enzymatic oxidation a supramolecular tripeptide in tyrosine 1D morphology demonstrated, retained during the process while conducting tracks form through oxidative crosslinking. Specifically, minimalistic self‐assembling peptide, Lys–Tyr–Tyr (KYY) strong propensity to fibers, utilized. Analysis Raman spectroscopy shows tyrosines pre‐organized inside fibers and, upon oxidation, result connected catechols. These along length fiber, which gives rise level internal disorder, but retention fiber morphology. This results highly conductive demonstrated be dominated proton conduction. work demonstrates ability control retain well‐defined fibrous does known equivalent biology, demonstrate exceptional conductivity enhanced oxidation.