Issue 3, 2021

Optical chemosensors for the detection of proximally phosphorylated peptides and proteins

Abstract

Proximal multi-site phosphorylation is a critical post-translational modification in protein biology. The additive effects of multiple phosphosite clusters in close spatial proximity triggers integrative and cooperative effects on protein conformation and activity. Proximal phosphorylation has been shown to modulate signal transduction pathways and gene expression, and as a result, is implicated in a broad range of disease states through altered protein function and/or localization including enzyme overactivation or protein aggregation. The role of proximal multi-phosphorylation events is becoming increasingly recognized as mechanistically important, although breakthroughs are limited due to a lack of detection technologies. To date, there is a limited selection of facile and robust sensing tools for proximal phosphorylation. Nonetheless, there have been considerable efforts in developing optical chemosensors for the detection of proximal phosphorylation motifs on peptides and proteins in recent years. This review provides a comprehensive overview of optical chemosensors for proximal phosphorylation, with the majority of work being reported in the past two decades. Optical sensors, in the form of fluorescent and luminescent chemosensors, hybrid biosensors, and inorganic nanoparticles, are described. Emphasis is placed on the rationale behind sensor scaffolds, relevant protein motifs, and applications in protein biology.

Graphical abstract: Optical chemosensors for the detection of proximally phosphorylated peptides and proteins

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Article information

Article type
Review Article
Submitted
16 mar 2021
Accepted
19 abr 2021
First published
21 abr 2021
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2021,2, 815-829

Optical chemosensors for the detection of proximally phosphorylated peptides and proteins

A. D. Cabral, T. B. Radu, E. D. de Araujo and P. T. Gunning, RSC Chem. Biol., 2021, 2, 815 DOI: 10.1039/D1CB00055A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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