Diacid Linkers That Promote Parallel β-Sheet Secondary Structure in Water

Abstract
We report the development of diacid units that promote formation of a two-stranded parallel β-sheet secondary structure between peptide segments attached via their N-termini. These linker units are formed by attaching glycine to one carboxyl group of cis-1,2-cyclohexanedicarboxylic acid (CHDA). Parallel sheet formation in water is observed when l-residue strands are attached to the CHDA-Gly unit with either of the two absolute configurations.