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 |
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Pages (from-to) | 8438-8442 |
Number of pages | 5 |
Journal | Organic and Biomolecular Chemistry |
Volume | 14 |
Issue number | 36 |
DOIs | |
Publication status | Published - 2016 |
Bibliographical note
Publisher Copyright:© 2014 The Royal Society of Chemistry.
All Science Journal Classification (ASJC) codes
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry