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A Schematic presentation of the assay concept: The universal RNA <t>MTase</t> co-product SAH binds to a FAM/TAMRA labeled split aptamer which can be investigated by microscale thermophoresis (MST) and FRET experimental setups. B Sequence and secondary structure model of the split aptamer consisting of 5′-TAMRA labeled aptaSAH1 (orange) and 3′-FAM labeled aptaSAH2 (cyan). C Dose-response curves of aptaSAH1&2 (each 50 nM) in the presence of the SAH or SAM ligand by plate reader-based FRET assays (λ ex = 485 nm; λ em = 600 nm). D Dose-response curves analogously to subfigure ( C ) but determined from MST experiments with variable concentrations of SAH and SAM titrated to the aptamer highlight the dynamic range of the assay scope (mean ± SD, n = 3). E Z-factor determination at 50 nM SAH ( n = 32) to evaluate the robustness of the assay setup. F MST traces of aptaSAH1&2 (each 50 nM) in the presence of the SAH ligand yielded significant thermophoresis shifts.
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A Schematic presentation of the assay concept: The universal RNA <t>MTase</t> co-product SAH binds to a FAM/TAMRA labeled split aptamer which can be investigated by microscale thermophoresis (MST) and FRET experimental setups. B Sequence and secondary structure model of the split aptamer consisting of 5′-TAMRA labeled aptaSAH1 (orange) and 3′-FAM labeled aptaSAH2 (cyan). C Dose-response curves of aptaSAH1&2 (each 50 nM) in the presence of the SAH or SAM ligand by plate reader-based FRET assays (λ ex = 485 nm; λ em = 600 nm). D Dose-response curves analogously to subfigure ( C ) but determined from MST experiments with variable concentrations of SAH and SAM titrated to the aptamer highlight the dynamic range of the assay scope (mean ± SD, n = 3). E Z-factor determination at 50 nM SAH ( n = 32) to evaluate the robustness of the assay setup. F MST traces of aptaSAH1&2 (each 50 nM) in the presence of the SAH ligand yielded significant thermophoresis shifts.
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A Schematic presentation of the assay concept: The universal RNA MTase co-product SAH binds to a FAM/TAMRA labeled split aptamer which can be investigated by microscale thermophoresis (MST) and FRET experimental setups. B Sequence and secondary structure model of the split aptamer consisting of 5′-TAMRA labeled aptaSAH1 (orange) and 3′-FAM labeled aptaSAH2 (cyan). C Dose-response curves of aptaSAH1&2 (each 50 nM) in the presence of the SAH or SAM ligand by plate reader-based FRET assays (λ ex = 485 nm; λ em = 600 nm). D Dose-response curves analogously to subfigure ( C ) but determined from MST experiments with variable concentrations of SAH and SAM titrated to the aptamer highlight the dynamic range of the assay scope (mean ± SD, n = 3). E Z-factor determination at 50 nM SAH ( n = 32) to evaluate the robustness of the assay setup. F MST traces of aptaSAH1&2 (each 50 nM) in the presence of the SAH ligand yielded significant thermophoresis shifts.

Journal: Communications Chemistry

Article Title: A microscale thermophoresis-based enzymatic RNA methyltransferase assay enables the discovery of DNMT2 inhibitors

doi: 10.1038/s42004-025-01439-9

Figure Lengend Snippet: A Schematic presentation of the assay concept: The universal RNA MTase co-product SAH binds to a FAM/TAMRA labeled split aptamer which can be investigated by microscale thermophoresis (MST) and FRET experimental setups. B Sequence and secondary structure model of the split aptamer consisting of 5′-TAMRA labeled aptaSAH1 (orange) and 3′-FAM labeled aptaSAH2 (cyan). C Dose-response curves of aptaSAH1&2 (each 50 nM) in the presence of the SAH or SAM ligand by plate reader-based FRET assays (λ ex = 485 nm; λ em = 600 nm). D Dose-response curves analogously to subfigure ( C ) but determined from MST experiments with variable concentrations of SAH and SAM titrated to the aptamer highlight the dynamic range of the assay scope (mean ± SD, n = 3). E Z-factor determination at 50 nM SAH ( n = 32) to evaluate the robustness of the assay setup. F MST traces of aptaSAH1&2 (each 50 nM) in the presence of the SAH ligand yielded significant thermophoresis shifts.

Article Snippet: HTRF MTase assays with the commercial AptaFluor SAH assay kit (BellBrook Labs) were performed as described in the manufacturer’s manual in 96-well format .

Techniques: Labeling, Microscale Thermophoresis, Sequencing

A Screening a library including 160 drug-like compounds resulted in the identification of ten potential hit compounds (green) with an F norm > 1000‰ (equals >80% inhibition). Initial hits were confirmed by triplicate validation (mean ± SD, n = 3). Positive reaction control: aptamer spiked with 1 µM SAH; negative control: aptamer mock-treated with DMSO. B Exemplary MST traces of the library’s first 80 compounds. C Orthogonal screening of the library by FP displacement experiments using FTAD as the fluorescent tracer. FP experiments reveal that only alexidine ( Cpd 3 , green) is binding to the SAH-binding site. D An inhibition selectivity panel was established by MST aptamer assays using the MTase assays described in this study and 500 µM of the respective hit compound. Only DNMT2 was inhibited significantly. E Alexidine’s ( Cpd 3 ) dose-response curves and K D determination by DNMT2 FP assays (mean ± SD, n = 3). F FP assays to confirm the reversibility of alexidine binding to DNMT2. The polarization of the DNMT2-FTAD complex (96 mP) is displaced in the presence of alexidine (5 mP) and can be effectively restored by analytical size-exclusion chromatography (92 mP). A second treatment with alexidine leads to a repeated FP displacement (4 mP). G Chemical structures of the identified DNMT2 hits.

Journal: Communications Chemistry

Article Title: A microscale thermophoresis-based enzymatic RNA methyltransferase assay enables the discovery of DNMT2 inhibitors

doi: 10.1038/s42004-025-01439-9

Figure Lengend Snippet: A Screening a library including 160 drug-like compounds resulted in the identification of ten potential hit compounds (green) with an F norm > 1000‰ (equals >80% inhibition). Initial hits were confirmed by triplicate validation (mean ± SD, n = 3). Positive reaction control: aptamer spiked with 1 µM SAH; negative control: aptamer mock-treated with DMSO. B Exemplary MST traces of the library’s first 80 compounds. C Orthogonal screening of the library by FP displacement experiments using FTAD as the fluorescent tracer. FP experiments reveal that only alexidine ( Cpd 3 , green) is binding to the SAH-binding site. D An inhibition selectivity panel was established by MST aptamer assays using the MTase assays described in this study and 500 µM of the respective hit compound. Only DNMT2 was inhibited significantly. E Alexidine’s ( Cpd 3 ) dose-response curves and K D determination by DNMT2 FP assays (mean ± SD, n = 3). F FP assays to confirm the reversibility of alexidine binding to DNMT2. The polarization of the DNMT2-FTAD complex (96 mP) is displaced in the presence of alexidine (5 mP) and can be effectively restored by analytical size-exclusion chromatography (92 mP). A second treatment with alexidine leads to a repeated FP displacement (4 mP). G Chemical structures of the identified DNMT2 hits.

Article Snippet: HTRF MTase assays with the commercial AptaFluor SAH assay kit (BellBrook Labs) were performed as described in the manufacturer’s manual in 96-well format .

Techniques: Inhibition, Control, Negative Control, Binding Assay, Size-exclusion Chromatography

Pathways and molecules involved in the pathogenesis of subretinal fibrosis

Journal: Neural Regeneration Research

Article Title: Subretinal fibrosis secondary to neovascular age-related macular degeneration: mechanisms and potential therapeutic targets

doi: 10.4103/NRR.NRR-D-23-01642

Figure Lengend Snippet: Pathways and molecules involved in the pathogenesis of subretinal fibrosis

Article Snippet: Pro-fibrotic , Transforming growth factor-β signaling pathway Wnt signaling pathway Phosphatidylinositol-3-kinase/Akt pathway Vascular endothelial growth factor/vascular endothelial growth factor receptor Platelet derived growth factor/platelet derived growth factor receptor-β Interleukin-6/interleukin-6 receptor Hypoxia-inducible factor-1α/p53/miRNA-34a/Klotho pathway MRTF-A-SRF pathway Connective tissue growth factor, fibroblast growth factor 2, platelet-activating factor receptor, Galectin-1, Yes-associated protein, adiponectin, methyltransferase-like 3, matrix metalloproteinase 12, peptidyl arginine deiminase-4, αB-Crystallin, Snail (SNIA1), cyclooxygenase-2, (pro)renin receptor, sphingosine-1-phosphate, γ-secretase.

Techniques: Derivative Assay