1. A general method to quantify ligand-driven oligomerization from fluorescence-based images
- Author
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Graeme Milligan, Michael R. Stoneman, Richard J. Ward, Ionel Popa, Valerica Raicu, John D. Pediani, Annie Eis, Dammar N. Badu, and Gabriel Biener
- Subjects
Agonist ,0303 health sciences ,General method ,biology ,medicine.drug_class ,Ligand ,Cell Biology ,Mass spectrometry ,Biochemistry ,Fluorescence ,03 medical and health sciences ,chemistry.chemical_compound ,Monomer ,chemistry ,Biophysics ,medicine ,biology.protein ,Secretin receptor ,Epidermal growth factor receptor ,Molecular Biology ,030304 developmental biology ,Biotechnology - Abstract
Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein–protein interactions.
- Published
- 2019
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