Issue 7, 2022

Exploration of α/β/γ-peptidomimetics design for BH3 helical domains

Abstract

Systematic incorporation of ring-constrained β- and γ-amino acid residues into α-helix mimetics engenders stable helical secondary structures. In this paper, functional α/β/γ-helical peptidomimetics were explored for mimicry of BH3 helical domains, Bim as a pioneering study. The Bim-based α/β/γ-peptides in an αγααβα-hexad repeat with five helical turns inhibited the interaction between Bak and Bcl-xL with excellent resistance towards proteolytic digestion. Further optimization of the α/β/γ-backbone strategy will considerably expand the utility of functional α/β/γ-peptidomimetics, in particular due to its prominent stability against proteolysis.

Graphical abstract: Exploration of α/β/γ-peptidomimetics design for BH3 helical domains

Supplementary files

Article information

Article type
Communication
Submitted
12 oct. 2021
Accepted
17 déc. 2021
First published
21 déc. 2021

Chem. Commun., 2022,58, 945-948

Author version available

Exploration of α/β/γ-peptidomimetics design for BH3 helical domains

Y. Shin and H. Yang, Chem. Commun., 2022, 58, 945 DOI: 10.1039/D1CC05758H

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