We report the development of diacid units that promote formation of a two-stranded parallel beta-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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2689375 | PMC |
| http://dx.doi.org/10.1021/ja802042c | DOI Listing |
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