A novel BRET-based binding assay for interaction studies of relaxin family peptide receptor 3 with its ligands View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-02-04

AUTHORS

Jia-Hui Wang, Xiao-Xia Shao, Meng-Jun Hu, Dian Wei, Ya-Li Liu, Zeng-Guang Xu, Zhan-Yun Guo

ABSTRACT

Relaxin family peptide receptor 3 (RXFP3) is an A-class G protein-coupled receptor that is implicated in the regulation of food intake and stress response upon activation by its cognate agonist relaxin-3. To study its interaction with various ligands, we developed a novel bioluminescence resonance energy transfer (BRET)-based binding assay using the brightest NanoLuc as an energy donor and a newly developed cyan-excitable orange fluorescent protein (CyOFP) as an energy acceptor. An engineered CyOFP without intrinsic cysteine residues but with an introduced cysteine at the C-terminus was overexpressed in Escherichia coli and chemically conjugated to the A-chain N-terminus of an easily labeled chimeric R3/I5 peptide via an intermolecular disulfide linkage. After the CyOFP-conjugated R3/I5 bound to a shortened human RXFP3 (removal of 33 N-terminal residues) fused with the NanoLuc reporter at the N-terminus, high BRET signals were detected. Saturation binding and real-time binding assays demonstrated that this BRET pair retained high binding affinity with fast association/dissociation. Using this BRET pair, binding potencies of various ligands with RXFP3 were conveniently measured through competition binding assays. Thus, the novel BRET-based binding assay facilitates interaction studies of RXFP3 with various ligands. The engineered CyOFP without intrinsic cysteine residues may also be applied to other BRET-based binding assays in future studies. More... »

PAGES

895-903

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00726-017-2387-4

DOI

http://dx.doi.org/10.1007/s00726-017-2387-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1083541237

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28161795


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