Abstract
Short α/β-peptides that consist of alternating l-α-amino acids and trans-2-aminocyclopentanecarboxylic acid are known to adopt both 11- and 14/15-helical conformations in solution. We report short α/β-depsipeptides containing (S)-lactic acid as the third residue from the N-terminus. The α/β-depsipeptide pentamers and heptamers adopt 14/15-helical conformations analogous to the α-helix in the crystal state and display 14/15-helical conformations predominantly in solution.
| Original language | English |
|---|---|
| Pages (from-to) | 8438-8442 |
| Number of pages | 5 |
| Journal | Organic and Biomolecular Chemistry |
| Volume | 14 |
| Issue number | 36 |
| DOIs | |
| Publication status | Published - 2016 Jan 1 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry
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Lee, J., Jang, G., Kang, P., Choi, M. G., & Choi, S. H. (2016). Helical α/β-depsipeptides with alternating residue types: Conformational change from the 11-helix to the 14/15-helix. Organic and Biomolecular Chemistry, 14(36), 8438-8442. https://doi.org/10.1039/c6ob01602b