The Experts below are selected from a list of 708375 Experts worldwide ranked by ideXlab platform
Amadeu Llebaria - One of the best experts on this subject based on the ideXlab platform.
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Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Analytical and bioanalytical chemistry, 2020Co-Authors: Maria Ricart-ortega, Alice E Berizzi, Juan Lorenzo Catena, Fanny Malhaire, Lourdes Muñoz, Carmen Serra, Guillaume Lebon, Cyril Goudet, Amadeu LlebariaAbstract: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.
Maria Ricart-ortega - One of the best experts on this subject based on the ideXlab platform.
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Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Analytical and bioanalytical chemistry, 2020Co-Authors: Maria Ricart-ortega, Alice E Berizzi, Juan Lorenzo Catena, Fanny Malhaire, Lourdes Muñoz, Carmen Serra, Guillaume Lebon, Cyril Goudet, Amadeu LlebariaAbstract: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.
Alice E Berizzi - One of the best experts on this subject based on the ideXlab platform.
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Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Analytical and bioanalytical chemistry, 2020Co-Authors: Maria Ricart-ortega, Alice E Berizzi, Juan Lorenzo Catena, Fanny Malhaire, Lourdes Muñoz, Carmen Serra, Guillaume Lebon, Cyril Goudet, Amadeu LlebariaAbstract: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.
Juan Lorenzo Catena - One of the best experts on this subject based on the ideXlab platform.
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Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Analytical and bioanalytical chemistry, 2020Co-Authors: Maria Ricart-ortega, Alice E Berizzi, Juan Lorenzo Catena, Fanny Malhaire, Lourdes Muñoz, Carmen Serra, Guillaume Lebon, Cyril Goudet, Amadeu LlebariaAbstract: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.
Fanny Malhaire - One of the best experts on this subject based on the ideXlab platform.
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Development and validation of a mass spectrometry binding assay for mGlu5 receptor
Analytical and bioanalytical chemistry, 2020Co-Authors: Maria Ricart-ortega, Alice E Berizzi, Juan Lorenzo Catena, Fanny Malhaire, Lourdes Muñoz, Carmen Serra, Guillaume Lebon, Cyril Goudet, Amadeu LlebariaAbstract: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.
