Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Mass spectrometry (MS) binding assays are a label-free alternative to radioligand or fluorescence binding assays, so the readout is based on direct mass spectrometric detection of the test ligand. The study presented here describes the development and validation of a highly sensitive, rapid, and rob...
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| Published in | Analytical and bioanalytical chemistry Vol. 412; no. 22; pp. 5525 - 5535 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
01.09.2020
Springer Springer Nature B.V Springer Verlag |
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| Online Access | Get full text |
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| Abstract | Mass spectrometry (MS) binding assays are a label-free alternative to radioligand or fluorescence binding assays, so the readout is based on direct mass spectrometric detection of the test ligand. The study presented here describes the development and validation of a highly sensitive, rapid, and robust MS binding assay for the quantification of the binding of the metabotropic glutamate 5 (mGlu5) negative allosteric modulator (NAM), MPEP (2-methyl-6-phenylethynylpyridine) at the mGlu5 allosteric binding site. The LC-ESI-MS/MS (liquid chromatography-electrospray ionization-tandem mass spectrometric) analytical method was established and validated with a deuterated analogue of MPEP as an internal standard. The developed MS binding assay described here allowed for the determination of MS binding affinity estimates that were in agreement with affinity estimates obtained from a tritiated MPEP radioligand saturation binding assay, indicating the suitability of this methodology for determining affinity estimates for compounds that target mGlu5 allosteric binding sites.
Graphical abstract |
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| AbstractList | Mass spectrometry (MS) binding assays are a label-free alternative to radioligand or fluorescence binding assays, so the readout is based on direct mass spectrometric detection of the test ligand. The study presented here describes the development and validation of a highly sensitive, rapid, and robust MS binding assay for the quantification of the binding of the metabotropic glutamate 5 (mGlu5) negative allosteric modulator (NAM), MPEP (2-methyl-6-phenylethynylpyridine) at the mGlu5 allosteric binding site. The LC-ESI-MS/MS (liquid chromatography-electrospray ionization-tandem mass spectrometric) analytical method was established and validated with a deuterated analogue of MPEP as an internal standard. The developed MS binding assay described here allowed for the determination of MS binding affinity estimates that were in agreement with affinity estimates obtained from a tritiated MPEP radioligand saturation binding assay, indicating the suitability of this methodology for determining affinity estimates for compounds that target mGlu5 allosteric binding sites. Mass spectrometry (MS) binding assays are a label-free alternative to radioligand or fluorescence binding assays, so the readout is based on direct mass spectrometric detection of the test ligand. The study presented here describes the development and validation of a highly sensitive, rapid, and robust MS binding assay for the quantification of the binding of the metabotropic glutamate 5 (mGlu5) negative allosteric modulator (NAM), MPEP (2-methyl-6-phenylethynylpyridine) at the mGlu5 allosteric binding site. The LC-ESI-MS/MS (liquid chromatography-electrospray ionization-tandem mass spectrometric) analytical method was established and validated with a deuterated analogue of MPEP as an internal standard. The developed MS binding assay described here allowed for the determination of MS binding affinity estimates that were in agreement with affinity estimates obtained from a tritiated MPEP radioligand saturation binding assay, indicating the suitability of this methodology for determining affinity estimates for compounds that target mGlu5 allosteric binding sites. Graphical abstract. Mass spectrometry (MS) binding assays are a label-free alternative to radioligand or fluorescence binding assays, so the readout is based on direct mass spectrometric detection of the test ligand. The study presented here describes the development and validation of a highly sensitive, rapid, and robust MS binding assay for the quantification of the binding of the metabotropic glutamate 5 (mGlu5) negative allosteric modulator (NAM), MPEP (2-methyl-6-phenylethynylpyridine) at the mGlu5 allosteric binding site. The LC-ESI-MS/MS (liquid chromatography-electrospray ionization-tandem mass spectrometric) analytical method was established and validated with a deuterated analogue of MPEP as an internal standard. The developed MS binding assay described here allowed for the determination of MS binding affinity estimates that were in agreement with affinity estimates obtained from a tritiated MPEP radioligand saturation binding assay, indicating the suitability of this methodology for determining affinity estimates for compounds that target mGlu5 allosteric binding sites. Graphical abstract |
| Audience | Academic |
| Author | Serra, Carmen Goudet, Cyril Muñoz, Lourdes Catena, Juanlo Berizzi, Alice E. Malhaire, Fanny Llebaria, Amadeu Ricart-Ortega, Maria Lebon, Guillaume |
| Author_xml | – sequence: 1 givenname: Maria surname: Ricart-Ortega fullname: Ricart-Ortega, Maria organization: MCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), IGF, CNRS, INSERM, University of Montpellier – sequence: 2 givenname: Alice E. surname: Berizzi fullname: Berizzi, Alice E. organization: IGF, CNRS, INSERM, University of Montpellier – sequence: 3 givenname: Juanlo surname: Catena fullname: Catena, Juanlo organization: MCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC) – sequence: 4 givenname: Fanny surname: Malhaire fullname: Malhaire, Fanny organization: IGF, CNRS, INSERM, University of Montpellier – sequence: 5 givenname: Lourdes surname: Muñoz fullname: Muñoz, Lourdes organization: MCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), SIMchem, Service of Synthesis of High Added Value Molecules, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC) – sequence: 6 givenname: Carmen surname: Serra fullname: Serra, Carmen organization: MCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), SIMchem, Service of Synthesis of High Added Value Molecules, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC) – sequence: 7 givenname: Guillaume surname: Lebon fullname: Lebon, Guillaume organization: IGF, CNRS, INSERM, University of Montpellier – sequence: 8 givenname: Cyril orcidid: 0000-0002-8255-3535 surname: Goudet fullname: Goudet, Cyril email: cyril.goudet@igf.cnrs.fr organization: IGF, CNRS, INSERM, University of Montpellier – sequence: 9 givenname: Amadeu orcidid: 0000-0002-8200-4827 surname: Llebaria fullname: Llebaria, Amadeu email: amadeu.llebaria@iqac.csic.es organization: MCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), SIMchem, Service of Synthesis of High Added Value Molecules, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC) |
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| Keywords | MS binding assays Saturation assay MPEP mGlu5 receptor Radioligand binding assays |
| Language | English |
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