Issue 7, 2022

Small molecule modulation of protein polymerization

Abstract

The modulation of protein surface physicochemistry through single point mutations can trigger polymerization, which is facilitated by subunit repetition within a homomeric complex. Furthermore, monogenic disorders may result from aberrant supramolecular assemblies caused by missense mutations that modify the protein surface. Noteworthy from a therapeutic perspective, small molecules have been shown to not only mediate and enhance polymerization, analogous to a surface residue perturbation, but also bind and stabilize the repeating unit to inhibit the self-assembly event. We exemplify pharmacological manipulation of polymeric protein assemblies using some recently reported studies. The aim of this Viewpoint is to highlight opportunities to rationally control protein polymerization for therapeutic benefit.

Graphical abstract: Small molecule modulation of protein polymerization

Article information

Article type
Viewpoint
Submitted
22 ene. 2022
First published
10 mar. 2022

Chem. Soc. Rev., 2022,51, 2392-2396

Small molecule modulation of protein polymerization

E. S. Fischer and L. H. Jones, Chem. Soc. Rev., 2022, 51, 2392 DOI: 10.1039/D2CS00070A

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