Journal of the American Chemical Society p. 7839 - 7841 (2008)
Update date:2022-08-04
Topics:
Freire, Felix
Fisk, John D.
Peoples, Aaron J.
Ivancic, Monika
Guzei, Ilia A.
Gellman, Samuel H.
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. Copyright
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