BRET (Bioluminescence Resonance Energy Transfer) is one of the key methods in studying PPI. While FRET is also quite popular, BRET is in many cases a better alternative, as it has a much lower background. BRET is very popular in the field of G-protein coupled receptor research which is very important in drug discovery: currently ~30 % of drugs are targeted against GPCRs, but only 5 % of the known receptors are targeted with drugs.

Other methods covered in our articles are HTRF® and Nano-BiT®, a commercial protein complementation assay.

Methods used to study protein-protein interactions are also useful to study protein trafficking: if a protein of interest interacts with a protein located, for example, in the plasmatic membrane, this indicates that it has been translocated to the plasmatic membrane. You can see examples of this approach in some of the publications below.

Microplate readers for BRET and more

We have been working closely with the BRET community since the introduction of our first multimode reader, the Mithras LB 940. Today the Tristar 3 continues this tradition, but at a fraction of the cost. This filter-based multimode reader measures absorbance, fluorescence and luminescence with great performance without breaking the bank. And, of course, filter sets are available for the most popular BRET assays!

Tristar 3 Multimode Reader

 

Selected publications

YearAuthorsJournalTitleRelevant methods
2021Bas Brouwers, Edson Mendes de Oliveira, Maria Marti-Solano, et al.Cell Reports

Human MC4R variants affect endocytosis, trafficking and dimerization revealing multiple cellular mechanisms involved in weight regulation

BRET (protein trafficking)
2021Shane C. Wright, Viktoriya Lukasheva, Christian Le Gouill, et al.PNAS

BRET-based effector membrane translocation assay monitors GPCR-promoted and endocytosis-mediated Gq activation at early endosomes

BRET (protein trafficking)
2020Jérôme Granel, Roxane Lemoine, Eric Morello, et al.Frontiers in Immunology

4C3 Human Monoclonal Antibody: A Proof of Concept for Non-pathogenic Proteinase 3 Anti-neutrophil Cytoplasmic Antibodies in Granulomatosis With Polyangiitis

HTRF®
2020Eline Pottiea, Peter Dedeckerb, Christophe P. StoveBiochemical Pharmacology

Identification of psychedelic new psychoactive substances (NPS) showing biased agonism at the 5-HT2AR through simultaneous use of β-arrestin 2 and miniGαq bioassays

NanoBiT®
2020Isra Al Zamel, Abdulrasheed Palakkott, Arshida Ashraf, et al.Frontiers in Pharmacology

Interplay Between Angiotensin II Type 1 Receptor and Thrombin Receptor Revealed by Bioluminescence Resonance Energy Transfer Assay

BRET
2019Soon Gang Choi, Julien Olivet, Patricia Cassonnet, et al.Nature Communications

Maximizing binary interactome mapping with a minimal number of assays

NanoLuc two-hybrid (N2H)
2019Alexandre Connolly, Brian J. Holleran, Élie Simard, et al.Biochemical Pharmacology

Interplay between intracellular loop 1 and helix VIII of the angiotensin II type 2 receptor controls its activation

BRET
2019Maja Susec, Milan Sencanski, Sanja Glisic, et al.Neuropharmacology

Functional characterization of β2-adrenergic and insulin receptor heteromers

BRET
2019Elise Wouters, Adrián R. Marín, James A.R. Dalton, et al.International Journal of Molecular Sciences

Distinct Dopamine D2 Receptor Antagonists Differentially Impact D2 Receptor Oligomerization

NanoBiT®
2018Matthieu Masureel, Yaozhong Zou, Louis-Philippe Picard, et al.Nature Chemical Biology

Structural insights into binding specificity, efficacy and bias of a β2AR partial agonist

BRET

 

BRET publications

BRET publication compilation

A compilation of scientific articles using Mithras or Tristar microplate readers for BRET.

EN | PDF | 511.6 KB

Download now
 

HTRF® is a registered trademark of Cisbio Bioassays.

NanoBiT® is a registered trademark of Promega Corporation.

More about Protein-Protein Interaction