4.6 Article

Helical folding of α/β-peptides containing β-amino acids with an eight-membered ring constraint

Journal

ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 12, Issue 17, Pages 2641-2644

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ob00266k

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Funding

  1. Basic Science Research Program through the National Research Foundation of Korea [2011-0015106]
  2. TJ Science Fellowship of POSCO TJ Park Foundation
  3. National Research Foundation of Korea [2011-0015106] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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alpha beta beta-Tripeptide that contains a cyclic beta-amino acid with an eight-membered ring, a cis-2-aminocyclooct-5-enecarboxylic acid (cis-ACOE) or a cis-2-aminocyclooctanecarboxylic acid (cis-ACOC) displayed an 11/9-helical turn in the crystal state. The related alpha/beta-peptide oligomers were shown to adopt 11/9-helical conformations in solution.

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