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A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules

A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules

Published on: March 10, 2017

Label-free functional selectivity assays.

Ann M Ferrie¹, Vasiliy Goral, Chaoming Wang

¹Biochemical Technologies, Science and Technology Division, Corning Incorporated, Corning, NY, 14831, USA.

Methods in Molecular Biology (Clifton, N.J.)

|January 8, 2015

Summary

This summary is machine-generated.

Quantifying ligand bias at G protein-coupled receptors (GPCRs) is challenging. This study introduces five label-free dynamic mass redistribution (DMR) methods to assess ligand bias for the beta-2 adrenergic receptor (β2AR), revealing distinct receptor behaviors.

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Area of Science:

Pharmacology
Biochemistry
Drug Discovery

Background:

G protein-coupled receptors (GPCRs) are major drug targets, with functional selectivity (biased agonism) offering improved efficacy and safety.
Quantifying ligand bias, a key aspect of functional selectivity, remains a significant challenge in GPCR drug development.

Purpose of the Study:

To develop and validate novel label-free dynamic mass redistribution (DMR) assays for quantifying ligand bias at the beta-2 adrenergic receptor (β2AR).
To explore diverse β2AR conformations and ligand-directed signaling pathways using multiparametric DMR analysis.

Main Methods:

Development of five distinct label-free dynamic mass redistribution (DMR) assay formats.
Utilizing conformational probes (e.g., catechol) and microfluidics for detailed receptor profiling.
Integration of chemical biology tools and probe-modulated cell systems for comprehensive analysis.

Main Results:

Multiparametric DMR profiling revealed divergent pharmacology among β2AR agonists.
Detection of multiple β2AR conformations using catechol as a probe.
Identification of ligand-directed receptor desensitization and biased antagonism through advanced DMR assays.

Conclusions:

The developed DMR approaches provide a robust platform for assessing ligand bias and characterizing GPCR pharmacology.
These methods enable the discovery of biased agonists and antagonists with potential for improved therapeutic profiles.
Understanding receptor conformations and signaling bias is crucial for rational drug design targeting GPCRs.