Issue 7, 2022

Helical sulfono-γ-AApeptides with predictable functions in protein recognition

Abstract

Sulfono-γ-AApeptides are a subset of possible sequence-specific foldamers that might be considered for the design of biomimetic drug molecular structures. Although they have been studied for a relatively short period of time, a number of structures and functions have been designed or discovered within this class of unnatural peptides. Examples of utilizing these sulfono-γ-AApeptides have demonstrated the potential that sulfono-γ-AApeptides can offer, however, to date, their application in biomedical sciences yet remains unexplored. This review mainly summarizes the helical folding conformations of sulfono-γ-AApeptides and their biological application as helical mimetics in medicinally relevant protein–protein interactions (PPIs) and assesses their potential for the mimicry of other α-helices for protein recognition in the future.

Graphical abstract: Helical sulfono-γ-AApeptides with predictable functions in protein recognition

Article information

Article type
Review Article
Submitted
15 Feb 2022
Accepted
21 Apr 2022
First published
20 May 2022
This article is Open Access
Creative Commons BY-NC license

RSC Chem. Biol., 2022,3, 805-814

Helical sulfono-γ-AApeptides with predictable functions in protein recognition

P. Sang, Y. Shi, L. Wei and J. Cai, RSC Chem. Biol., 2022, 3, 805 DOI: 10.1039/D2CB00049K

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements