Abstract
α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.
| Original language | English |
|---|---|
| Pages (from-to) | 5950-5952 |
| Number of pages | 3 |
| Journal | Chemical Communications |
| Volume | 52 |
| Issue number | 35 |
| DOIs | |
| Publication status | Published - 2016 May 1 |
All Science Journal Classification (ASJC) codes
- Catalysis
- Electronic, Optical and Magnetic Materials
- Ceramics and Composites
- Chemistry(all)
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry
Fingerprint Dive into the research topics of 'Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents'. Together they form a unique fingerprint.
Cite this
Lee, M., Shim, J., Kang, P., Choi, M. G., & Choi, S. H. (2016). Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents. Chemical Communications, 52(35), 5950-5952. https://doi.org/10.1039/c6cc01189f