Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix
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Updated: Mar 16, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
Jaeyeon Lee1, Geunhyeok Jang, Philjae Kang
1Department of Chemistry, Yonsei University, Seoul, 03722, Republic of Korea. sh-choi@yonsei.ac.kr.
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.
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