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A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells

Fluorescent ligands for G-protein coupled receptors (GPCRs) are valuable tools for studying the expression, pharmacology and modulation of these therapeutically important proteins in living cells. Here we report a fluorescent photoaffinity probe for Formyl peptide receptor 1 (FPR1), a critical compo...

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Detalles Bibliográficos
Autores principales: Field, Devon H., White, Jack S., Warriner, Stuart L., Wright, Megan H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9994102/
https://www.ncbi.nlm.nih.gov/pubmed/36908701
http://dx.doi.org/10.1039/d2cb00199c
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author Field, Devon H.
White, Jack S.
Warriner, Stuart L.
Wright, Megan H.
author_facet Field, Devon H.
White, Jack S.
Warriner, Stuart L.
Wright, Megan H.
author_sort Field, Devon H.
collection PubMed
description Fluorescent ligands for G-protein coupled receptors (GPCRs) are valuable tools for studying the expression, pharmacology and modulation of these therapeutically important proteins in living cells. Here we report a fluorescent photoaffinity probe for Formyl peptide receptor 1 (FPR1), a critical component of the innate immune response to bacterial infection and a promising target in inflammatory diseases. We demonstrate that the probe binds and covalently crosslinks to FPR1 with good specificity at nanomolar concentrations in living cells and is a useful tool for visualisation and characterisation of this receptor.
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spelling pubmed-99941022023-03-09 A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells Field, Devon H. White, Jack S. Warriner, Stuart L. Wright, Megan H. RSC Chem Biol Chemistry Fluorescent ligands for G-protein coupled receptors (GPCRs) are valuable tools for studying the expression, pharmacology and modulation of these therapeutically important proteins in living cells. Here we report a fluorescent photoaffinity probe for Formyl peptide receptor 1 (FPR1), a critical component of the innate immune response to bacterial infection and a promising target in inflammatory diseases. We demonstrate that the probe binds and covalently crosslinks to FPR1 with good specificity at nanomolar concentrations in living cells and is a useful tool for visualisation and characterisation of this receptor. RSC 2023-01-13 /pmc/articles/PMC9994102/ /pubmed/36908701 http://dx.doi.org/10.1039/d2cb00199c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Field, Devon H.
White, Jack S.
Warriner, Stuart L.
Wright, Megan H.
A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title_full A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title_fullStr A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title_full_unstemmed A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title_short A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
title_sort fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9994102/
https://www.ncbi.nlm.nih.gov/pubmed/36908701
http://dx.doi.org/10.1039/d2cb00199c
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