Harnessing prion-inspired amyloid self-assembly for sustainable and biocompatible proton conductivity.

Protein-based materials have emerged as promising candidates for proton-conducting biomaterials. Therefore, drawing inspiration from the amino acid composition of prion-like domains, we designed short self-assembling peptides incorporating the (X-Tyr) motif, with X representing Asn, Gly and Ser, which form fibrillar structures capable of conducting protons. In this study, we conducted an analysis of the conductivity capacity of these fibers, with a focus on temperature and frequency dependence of conductivity. The loss tangent curves data and the electrode polarization model with the Debye approximation were employed to calculate transport properties, including conductivity, diffusivity, and density of charge carriers. Results revealed the prion-like fibers can transport protons more efficiently than biomaterials and other synthetic proton conducting materials, and that a significant increase in conductivity is observed with fibrillar orientations. The temperature dependence of conductivity of the peptides, measured in wet conditions, showed conductivities following the trend