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Updated: May 14, 2025

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
Stereochemical matching determines both helix type and handedness in α/γ-peptides with a cyclic-constrained γ-amino
Dayi Liu1, Ali T Mansour1,2, Ogaritte Yazbeck2
1Université Paris-Saclay, CNRS, ICMMO, 91400 Orsay, France. david.aitken@universite-paris-saclay.fr.
Abstract:
The folding preferences of α/γ-peptides containing a bespoke chiral cyclobutane-constrained γ-amino acid have been examined in a low-polarity solvent by quantum chemical calculations. With (S)-alanine, the preferred conformation is a right-handed 12/10 helix, whereas with (R)-alanine a left-handed 12 helical architecture is promoted. Experimental evidence for this dichotomy was obtained by detailed analysis of the IR amide I and II absorption bands and their assignments with assistance from theoretical simulations.
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