Structural characterization of peptide oligomers containing (1R,2S)-2-aminocyclohexanecarboxylic acid (cis-ACHC)

Soo Hyuk Choi, Monika Ivancic, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

(1R,2S)-2-Aminocyclohexanecarboxylic acid (cis-ACHC) is a preorganized β-amino acid. cis-ACHC favors two conformations that feature gauche conformations about the Cα-Cβ bond with torsion angles of opposite signs. The diastereomeric β-amino acid trans-ACHC has been widely studied as a foldamer building block, but cis-ACHC has received less attention in this regard. We examined the conformational behaviour of three types of oligomer: (1) homooligomers of cis-ACHC, (2) β-peptides in which cis-ACHC and β3h-Ala alternate, and (3) 1:1 α/β- peptides in which cis-ACHC and Ala alternate. Two-dimensional NMR experiments suggest that all three types of oligomer adopt extended conformations rather than folded conformations in solution. Two crystal structures of oligomers that contain cis-ACHC residues, a cis-ACHC dimer and an α/β-peptide tetramer, show extended conformations in which the cis-ACHC residues contain six-membered-ring C=O⋯H-N hydrogen bonds.

Original languageEnglish
Pages (from-to)3464-3469
Number of pages6
JournalEuropean Journal of Organic Chemistry
Issue number17
DOIs
Publication statusPublished - 2013 Jun

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Organic Chemistry

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