Issue 28, 2022

Peptide and protein chemistry approaches to study the tumor suppressor protein p53

Abstract

The tumor suppressor and master gene regulator protein p53 has been the subject of intense investigation for several decades due to its mutation in about half of all human cancers. However, mechanistic studies of p53 in cells are complicated by its many dynamic binding partners and heterogeneous post-translational modifications. The design of therapeutics that rescue p53 functions in cells requires a mechanistic understanding of its protein–protein interactions in specific protein complexes and identifying changes in p53 activity by diverse post-translational modifications. This review highlights the important roles that peptide and protein chemistry have played in biophysical and biochemical studies aimed at elucidating p53 regulation by several key binding partners. The design of various peptide inhibitors that rescue p53 function in cells and new opportunities in targeting p53-protein interactions are discussed. In addition, the review highlights the importance of a protein semisynthesis approach to comprehend the role of site-specific PTMs in p53 regulation.

Graphical abstract: Peptide and protein chemistry approaches to study the tumor suppressor protein p53

Article information

Article type
Review Article
Submitted
12 May 2022
Accepted
28 Jun 2022
First published
29 Jun 2022

Org. Biomol. Chem., 2022,20, 5500-5509

Author version available

Peptide and protein chemistry approaches to study the tumor suppressor protein p53

C. Chatterjee and S. K. Singh, Org. Biomol. Chem., 2022, 20, 5500 DOI: 10.1039/D2OB00902A

To request permission to reproduce material from this article, 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 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