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Issue 36, 2016
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Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix

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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.

Graphical abstract: Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix

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Article information


Submitted
27 Jul 2016
Accepted
10 Aug 2016
First published
11 Aug 2016

Org. Biomol. Chem., 2016,14, 8438-8442
Article type
Communication

Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix

J. Lee, G. Jang, P. Kang, M. Choi and S. H. Choi, Org. Biomol. Chem., 2016, 14, 8438
DOI: 10.1039/C6OB01602B

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