Selective Peptide Binders to the Perfluorinated Sulfonic Acid Ionomer Nafion

Abstract

AbstractFuel cells used for transport applications hold polymer membranes as a key element. Their efficiency can be significantly increased if structured ion channels are implemented at the molecular level into the proton‐conducting membrane. New functional molecules with selective affinity for ionomers are needed to obtain such a membrane design. This study presents a method to screen for selective peptide binders to perfluorinated sulfonic acid ionomers, e.g., Nafion using ultra‐high density peptide arrays with a spot size of up to 30 µm. First, the ionomer dispersion is incubated with the peptide chip containing 56014 randomly chosen 6‐mer peptides. Afterward, the peptide chip is washed. The peptide WIWHCW with the helix structure is identified as a selective binder to Nafion. The invariant amino acids responsible for binding are also determined using a peptide chip approach. The specific binding pocket of WIWHCW is formed by histidine and tryptophan. Its dissociation constant to the ionomer is measured at ≈140 µM.