Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents?

Chemical Communications Pub Date: 2016-03-30 DOI: 10.1039/C6CC01189F

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.

Graphical abstract: Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents
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