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Related Experiment Video

Updated: May 31, 2026

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay

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Screening for GPCR Ligands Using Surface Plasmon Resonance.

Iva Navratilova¹, Jérémy Besnard, Andrew L Hopkins

¹Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee , Dundee, DD1 5EH, United Kingdom.

ACS Medicinal Chemistry Letters

|July 19, 2011

Summary

This summary is machine-generated.

A novel biosensor assay directly measures G-protein coupled receptor (GPCR)-ligand interactions. This label-free, cell-free method overcomes limitations of traditional assays, enabling efficient screening for new drug candidates like CCR5 ligands.

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Area of Science:

Pharmacology
Biochemistry
Drug Discovery

Background:

G-protein coupled receptors (GPCRs) are critical drug targets.
Current assays indirectly measure ligand binding through displacement or functional responses.
Challenges include allosteric modulation, probe dependence, and functional selectivity.

Purpose of the Study:

To develop a direct, label-free method for measuring GPCR-ligand interactions.
To overcome limitations of indirect and displacement-based screening assays.
To enable high-throughput screening for novel GPCR ligands.

Main Methods:

Developed a GPCR biosensor assay protocol.
Utilized label-free, cell-free screening.
Applied the method to solubilized, native GPCRs.

Main Results:

Successfully identified interactions of orthosteric and allosteric ligands.
Demonstrated the assay's ability to screen in a label-free, cell-free environment.
Exemplified the method by discovering novel ligands for the chemokine receptor CCR5.

Conclusions:

The GPCR biosensor assay provides a direct, label-free method for screening GPCR-ligand interactions.
This approach overcomes limitations of conventional assays.
It facilitates the discovery of novel ligands, including fragment-based leads for targets like CCR5.