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Tahk, Maris-Johanna ; Torp, Jane ; Ali, Mohammed A. S. ; Fishman, Dmytro ; Parts, Leopold ; Grätz, Lukas ; Müller, Christoph ; Keller, Max ; Veiksina, Santa ; Laasfeld, Tõnis ; Rinken, Ago

Live-cell microscopy or fluorescence anisotropy with budded baculoviruses—which way to go with measuring ligand binding to M 4 muscarinic receptors?

Article

Tahk, Maris-Johanna , Torp, Jane , Ali, Mohammed A. S. , Fishman, Dmytro, Parts, Leopold , Grätz, Lukas , Müller, Christoph , Keller, Max , Veiksina, Santa , Laasfeld, Tõnis and Rinken, Ago (2022) Live-cell microscopy or fluorescence anisotropy with budded baculoviruses—which way to go with measuring ligand binding to M 4 muscarinic receptors? Open Biology 12 (6).

DOI to cite this document: 10.5283/epub.57457


Abstract

M-4 muscarinic acetylcholine receptor is a G protein-coupled receptor (GPCR) that has been associated with alcohol and cocaine abuse, Alzheimer's disease, and schizophrenia which makes it an interesting drug target. For many GPCRs, the high-affinity fluorescence ligands have expanded the options for high-throughput screening of drug candidates and serve as useful tools in fundamental receptor ...

M-4 muscarinic acetylcholine receptor is a G protein-coupled receptor (GPCR) that has been associated with alcohol and cocaine abuse, Alzheimer's disease, and schizophrenia which makes it an interesting drug target. For many GPCRs, the high-affinity fluorescence ligands have expanded the options for high-throughput screening of drug candidates and serve as useful tools in fundamental receptor research. Here, we explored two TAMRA-labelled fluorescence ligands, UR-MK342 and UR-CG072, for development of assays for studying ligand-binding properties to M-4 receptor. Using budded baculovirus particles as M-4 receptor preparation and fluorescence anisotropy method, we measured the affinities and binding kinetics of both fluorescence ligands. Using the fluorescence ligands as reporter probes, the binding affinities of unlabelled ligands could be determined. Based on these results, we took a step towards a more natural system and developed a method using live CHO-K1-hM(4)R cells and automated fluorescence microscopy suitable for the routine determination of unlabelled ligand affinities. For quantitative image analysis, we developed random forest and deep learning-based pipelines for cell segmentation. The pipelines were integrated into the user-friendly open-source Aparecium software. Both image analysis methods were suitable for measuring fluorescence ligand saturation binding and kinetics as well as for screening binding affinities of unlabelled ligands.



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Details

Item typeArticle
Journal or Publication TitleOpen Biology
PublisherThe Royal Society publishing
Open Access TypeCC-License
Place of PublicationLONDON
Volume12
Number of Issue or Book Chapter6
Date2022
Date of publication29 Feb 2024 12:56
InstitutionsChemistry and Pharmacy > Institute of Pharmacy
Identification Number
ValueType
10.1098/rsob.220019DOI
KeywordsPROTEIN-COUPLED RECEPTORS; PHARMACOLOGICAL CHARACTERIZATION; ACETYLCHOLINE-RECEPTORS; SUBTYPES; ASSAY; ANTAGONIST; M1; M4; SELECTIVITY; AFFINITY; fluorescence anisotropy; microscopy; G protein-coupled receptor; muscarinic acetylcholine M-4 receptor; fluorescent ligands; deep learning
Dewey Decimal Classification600 Technology > 615 Pharmacy
StatusPublished
RefereedYes, this version has been refereed
Created at the University of RegensburgYes
URN of the UB Regensburgurn:nbn:de:bvb:355-epub-574578
Item ID57457

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