Stereochemical matching determines both helix type and handedness in α/γ-peptides with a cyclic-constrained γ-amino acid
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 (<i>S</i>)-alanine, the preferred conformation is a right-handed 12/10 helix, whereas with (<i>R</i>)-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.
Authors
- Eric Gloaguen (ORCID: https://orcid.org/0000-0002-1023-2791)
- Valérie Brenner (ORCID: https://orcid.org/0000-0002-8004-1157)
- Dayi Liu (ORCID: https://orcid.org/0000-0002-0251-6399)
- Sylvie Robin (ORCID: https://orcid.org/0000-0003-3450-1412)
- Daoud Naoufal (ORCID: https://orcid.org/0000-0003-3685-9100)
- David J. Aitken (ORCID: https://orcid.org/0000-0002-5164-6042)
- Ogaritte Yazbeck
- Ali Mansour
- Michel Mons (ORCID: https://orcid.org/0000-0001-9930-831X)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Lebanese University (LB)
- Université Paris Cité (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Université Paris-Saclay (FR)
- Sorbonne Paris Cité (FR)
- Institut Rayonnement-Matière de Saclay (FR)
- Institut des Sciences Moléculaires d'Orsay (FR)
- CEA Paris-Saclay (FR)
- Institut de Chimie Moléculaire et des Matériaux d'Orsay (FR)
- Laboratoire Interactions, Dynamiques et Lasers (FR)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5cc00746a
- Citations
- 1
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.81