| Literature DB >> 18507461 |
Felix Freire1, John D Fisk, Aaron J Peoples, Monika Ivancic, Ilia A Guzei, Samuel H Gellman.
Abstract
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.Entities:
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Year: 2008 PMID: 18507461 PMCID: PMC2689375 DOI: 10.1021/ja802042c
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419