Abstract
Anti-β2,3-amino acids are a class of acyclic β-amino acids that usually stabilize β-sheet-like conformations of unnatural peptides. (2S,3R)-3-amino-2-ethylpentanoic acid (AEPA) is a diethyl-substituted anti-β2,3-amino acid that can be regarded as an acyclic analog of cis-2-aminocyclohexanecarboxylic acid, which is known to promote the α/β-peptide 11/9-helix and the β-peptide 12/10-helix. We report that AEPA can be incorporated into the two unnatural peptide helices without disrupting helical folding. Crystal structure data reveal that the anti-β2,3-residue adopts unconventional gauche (+) conformation in those unnatural peptide helices.
Original language | English |
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Pages (from-to) | 241-245 |
Number of pages | 5 |
Journal | Bulletin of the Korean Chemical Society |
Volume | 43 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2022 Feb |
Bibliographical note
Funding Information:Korea Health Industry Development Institute; Korea Health Technology R&D Project, Grant/Award Number: HI20C0026; National Research Foundation of Korea, Grant/Award Number: NRF‐2021R1A2C1013477 Funding information
Funding Information:
This study was supported in part by the National Research Foundation of Korea (NRF‐2021R1A2C1013477) and by the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (grant number: HI20C0026). The high‐field NMR data and the crystal structure data were acquired at the Korea Basic Science Institute (Western Seoul).
Funding Information:
This study was supported in part by the National Research Foundation of Korea (NRF-2021R1A2C1013477) and by the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (grant number: HI20C0026). The high-field NMR data and the crystal structure data were acquired at the Korea Basic Science Institute (Western Seoul).
Publisher Copyright:
© 2021 Korean Chemical Society, Seoul & Wiley-VCH GmbH.
All Science Journal Classification (ASJC) codes
- Chemistry(all)