Issue 35, 2016
From the journal:

Chemical Communications

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

Mihye Lee,a   Jihyun Shim,a   Philjae Kang,a   Moon-Gun Choia  and  Soo Hyuk Choi*a  

* Corresponding authors

a Department of Chemistry, Yonsei University, Seoul, Republic of Korea
E-mail: sh-choi@yonsei.ac.kr

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

  • This article is part of the themed collection: Foldamers
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Article information

DOI
https://doi.org/10.1039/C6CC01189F
Article type
Communication
Submitted
05 févr. 2016
Accepted
30 mars 2016
First published
30 mars 2016

Chem. Commun., 2016,52, 5950-5952

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

M. Lee, J. Shim, P. Kang, M. Choi and S. H. Choi, Chem. Commun., 2016, 52, 5950 DOI: 10.1039/C6CC01189F

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