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 |
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Pages (from-to) | 5950-5952 |
Number of pages | 3 |
Journal | Chemical Communications |
Volume | 52 |
Issue number | 35 |
DOIs | |
Publication status | Published - 2016 May 1 |
Bibliographical note
Funding Information:This study was supported by the Basic Science Research Program (NRF-2014R1A1A2053841) and the BK21 plus program through the National Research Foundation of Korea.
Publisher Copyright:
© The Royal Society of Chemistry 2016.
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