Issue 8, 2024

The influence of backbone fluorination on the helicity of α/γ-hybrid peptides

Abstract

Peptides that are composed of an alternating pattern of α- and γ-amino acids are potentially valuable as metabolism-resistant bioactive agents. For optimal function, some kind of conformational restriction is usually required to either stabilize the dominant 12-helix, or else to divert the peptide away from this conformation in a controlled way. Herein, we explore stereoselective fluorination as a method for controlling the conformations of α/γ-hybrid peptides. We show through a combination of X-ray, NMR and CD analyses that fluorination can either stabilize or disrupt the 12-helix, depending on the fluorine stereochemistry. These findings could inform the ongoing development of diverse functional hybrid peptides.

Graphical abstract: The influence of backbone fluorination on the helicity of α/γ-hybrid peptides

Supplementary files

Article information

Article type
Communication
Submitted
10 Dec 2023
Accepted
23 Jan 2024
First published
31 Jan 2024

Org. Biomol. Chem., 2024,22, 1608-1612

The influence of backbone fluorination on the helicity of α/γ-hybrid peptides

A. R. Patel, A. Lawer, M. Bhadbhade and L. Hunter, Org. Biomol. Chem., 2024, 22, 1608 DOI: 10.1039/D3OB02016A

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