Optical chemosensors for the detection of proximally phosphorylated peptides and proteins.

Autor:	Cabral AD; Department of Chemical and Physical Sciences, University of Toronto Mississauga 3359 Mississauga Road Mississauga Ontario L5L 1C6 Canada patrick.gunning@utoronto.ca.; Department of Chemistry, University of Toronto 80 St George Street Toronto Ontario M5S 3H6 Canada., Radu TB; Department of Chemical and Physical Sciences, University of Toronto Mississauga 3359 Mississauga Road Mississauga Ontario L5L 1C6 Canada patrick.gunning@utoronto.ca.; Department of Chemistry, University of Toronto 80 St George Street Toronto Ontario M5S 3H6 Canada., de Araujo ED; Department of Chemical and Physical Sciences, University of Toronto Mississauga 3359 Mississauga Road Mississauga Ontario L5L 1C6 Canada patrick.gunning@utoronto.ca., Gunning PT; Department of Chemical and Physical Sciences, University of Toronto Mississauga 3359 Mississauga Road Mississauga Ontario L5L 1C6 Canada patrick.gunning@utoronto.ca.; Department of Chemistry, University of Toronto 80 St George Street Toronto Ontario M5S 3H6 Canada.
Jazyk:	angličtina
Zdroj:	RSC chemical biology [RSC Chem Biol] 2021 Apr 21; Vol. 2 (3), pp. 815-829. Date of Electronic Publication: 2021 Apr 21 (Print Publication: 2021).
DOI:	10.1039/d1cb00055a
Abstrakt:	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. Competing Interests: There are no conflicts to declare. (This journal is © The Royal Society of Chemistry.)
Databáze:	MEDLINE
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