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a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and <t>cytochalasin</t> <t>B</t> (CyB).
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a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and <t>cytochalasin</t> <t>B</t> (CyB).
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a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and <t>cytochalasin</t> <t>B</t> (CyB).
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a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and <t>cytochalasin</t> <t>B</t> (CyB).
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Small molecules modulate SDH enzyme activity by direct binding.( a ) Flow chart demonstrating the small molecule selection process and research design. 94 small molecules targeting SDH and DMSO (n=2) were initially gathered by screening with the AtomNet model. Subsequently, single-blinded screening with mitochondria- and cell-based SDH activity and cell viability assays were performed, and two hit small molecules were shortlisted for additional characterization. ( b ) Plot depicting effects of small molecules on absolute and relative SDH enzyme activities in isolated mitochondria from AALE cells. The relative SDH activities of all tested small molecules (x-axis) were normalized to those treated with PBS. N = 2 replicates. ( c ) Chemical structures of H2/Z14 and C6/Z96. ( d ) Relative quantification of per cell SDH activity modulation by small molecules (H2/Z14, C6/Z96, and DMM) in H358 cells treated at 50 µM for four hours. N = 4 replicates. ( e,f ) Relative quantification of intracellular succinate levels in H1975 cells treated either 22 hours in a dose-dependent manner or at 30 µM in a time-dependent manner with small molecules H2/Z14 (d) or C6/Z96 (e). N=3 replicates.( g , h ) Thermal shift assay by western blotting for SDHA ( f ) and <t>SDHD</t> ( g ) in H358 cells treated with or without small molecules H2/Z14, C6/Z96, and DMM at 30 µM for 15 minutes. Melting temperature (Tm) was calculated using nonlinear regression analysis. N = 3 replicates . Data are mean± s.e.m. and were analyzed with Welch’s t -test ( c ) and one-way ANOVA ( d , e ). *, p <0.05; **, p <0.01; ***, p <0.001, ****, p <0.0001, ns, not significant
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Small molecules modulate SDH enzyme activity by direct binding.( a ) Flow chart demonstrating the small molecule selection process and research design. 94 small molecules targeting SDH and DMSO (n=2) were initially gathered by screening with the AtomNet model. Subsequently, single-blinded screening with mitochondria- and cell-based SDH activity and cell viability assays were performed, and two hit small molecules were shortlisted for additional characterization. ( b ) Plot depicting effects of small molecules on absolute and relative SDH enzyme activities in isolated mitochondria from AALE cells. The relative SDH activities of all tested small molecules (x-axis) were normalized to those treated with PBS. N = 2 replicates. ( c ) Chemical structures of H2/Z14 and C6/Z96. ( d ) Relative quantification of per cell SDH activity modulation by small molecules (H2/Z14, C6/Z96, and DMM) in H358 cells treated at 50 µM for four hours. N = 4 replicates. ( e,f ) Relative quantification of intracellular succinate levels in H1975 cells treated either 22 hours in a dose-dependent manner or at 30 µM in a time-dependent manner with small molecules H2/Z14 (d) or C6/Z96 (e). N=3 replicates.( g , h ) Thermal shift assay by western blotting for SDHA ( f ) and <t>SDHD</t> ( g ) in H358 cells treated with or without small molecules H2/Z14, C6/Z96, and DMM at 30 µM for 15 minutes. Melting temperature (Tm) was calculated using nonlinear regression analysis. N = 3 replicates . Data are mean± s.e.m. and were analyzed with Welch’s t -test ( c ) and one-way ANOVA ( d , e ). *, p <0.05; **, p <0.01; ***, p <0.001, ****, p <0.0001, ns, not significant
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Image Search Results


a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and cytochalasin B (CyB).

Journal: Small Science

Article Title: Biodegradable Aurum: Gold Nanosheets Undergo Biodegradation by Neutrophil Myeloperoxidase

doi: 10.1002/smsc.202500491

Figure Lengend Snippet: a) Shows an HR‐TEM image of AuNS along with the SAED pattern (inset). b) UV–vis–NIR spectrum of AuNS dispersed in water, c) Digital photos of AuNS dispersed in water and PBS for 2 days, respectively. d) Schematic shows the test‐tube model for biodegradation of AuNS by hMPO, and e) scheme for the in vitro degradation of AuNS using neutrophil‐like HL‐60 cells for 14 days, secreting MPO after activation with N‐formyl‐methionyl‐leucyl‐phenylalanine ( fMLP ) and cytochalasin B (CyB).

Article Snippet: 3‐(4,5‐dimethylthiazol‐2‐yl)‐2,5‐diphenyltetrazolium bromide (MTT) dye, calcein‐AM, propidium iodide (PI), N‐formyl‐methionyl‐leucylphenylalanine ( fMLP ) and cytochalasin B (CyB) were purchased from Invitrogen.

Techniques: In Vitro, Activation Assay

Small molecules modulate SDH enzyme activity by direct binding.( a ) Flow chart demonstrating the small molecule selection process and research design. 94 small molecules targeting SDH and DMSO (n=2) were initially gathered by screening with the AtomNet model. Subsequently, single-blinded screening with mitochondria- and cell-based SDH activity and cell viability assays were performed, and two hit small molecules were shortlisted for additional characterization. ( b ) Plot depicting effects of small molecules on absolute and relative SDH enzyme activities in isolated mitochondria from AALE cells. The relative SDH activities of all tested small molecules (x-axis) were normalized to those treated with PBS. N = 2 replicates. ( c ) Chemical structures of H2/Z14 and C6/Z96. ( d ) Relative quantification of per cell SDH activity modulation by small molecules (H2/Z14, C6/Z96, and DMM) in H358 cells treated at 50 µM for four hours. N = 4 replicates. ( e,f ) Relative quantification of intracellular succinate levels in H1975 cells treated either 22 hours in a dose-dependent manner or at 30 µM in a time-dependent manner with small molecules H2/Z14 (d) or C6/Z96 (e). N=3 replicates.( g , h ) Thermal shift assay by western blotting for SDHA ( f ) and SDHD ( g ) in H358 cells treated with or without small molecules H2/Z14, C6/Z96, and DMM at 30 µM for 15 minutes. Melting temperature (Tm) was calculated using nonlinear regression analysis. N = 3 replicates . Data are mean± s.e.m. and were analyzed with Welch’s t -test ( c ) and one-way ANOVA ( d , e ). *, p <0.05; **, p <0.01; ***, p <0.001, ****, p <0.0001, ns, not significant

Journal: Cancer Cell International

Article Title: Efficient identification of new small molecules targeting succinate dehydrogenase in non-small cell lung cancer

doi: 10.1186/s12935-025-04002-7

Figure Lengend Snippet: Small molecules modulate SDH enzyme activity by direct binding.( a ) Flow chart demonstrating the small molecule selection process and research design. 94 small molecules targeting SDH and DMSO (n=2) were initially gathered by screening with the AtomNet model. Subsequently, single-blinded screening with mitochondria- and cell-based SDH activity and cell viability assays were performed, and two hit small molecules were shortlisted for additional characterization. ( b ) Plot depicting effects of small molecules on absolute and relative SDH enzyme activities in isolated mitochondria from AALE cells. The relative SDH activities of all tested small molecules (x-axis) were normalized to those treated with PBS. N = 2 replicates. ( c ) Chemical structures of H2/Z14 and C6/Z96. ( d ) Relative quantification of per cell SDH activity modulation by small molecules (H2/Z14, C6/Z96, and DMM) in H358 cells treated at 50 µM for four hours. N = 4 replicates. ( e,f ) Relative quantification of intracellular succinate levels in H1975 cells treated either 22 hours in a dose-dependent manner or at 30 µM in a time-dependent manner with small molecules H2/Z14 (d) or C6/Z96 (e). N=3 replicates.( g , h ) Thermal shift assay by western blotting for SDHA ( f ) and SDHD ( g ) in H358 cells treated with or without small molecules H2/Z14, C6/Z96, and DMM at 30 µM for 15 minutes. Melting temperature (Tm) was calculated using nonlinear regression analysis. N = 3 replicates . Data are mean± s.e.m. and were analyzed with Welch’s t -test ( c ) and one-way ANOVA ( d , e ). *, p <0.05; **, p <0.01; ***, p <0.001, ****, p <0.0001, ns, not significant

Article Snippet: Fig. 4 H2/Z14 and C6/Z96 modulate SDH subunit protein abundance. ( a ) Normalized expression of SDHA , SDHB , SDHC , and SDHD across human lung adenocarcinoma (LUAD, N=80) and immortalized lung epithelial & fibroblast cell lines (Lung, N=8) from the Human Protein Atlas database.

Techniques: Activity Assay, Binding Assay, Selection, Isolation, Quantitative Proteomics, Thermal Shift Assay, Western Blot

H2/Z14 and C6/Z96 modulate SDH subunit protein abundance.( a ) Normalized expression of SDHA , SDHB , SDHC , and SDHD across human lung adenocarcinoma (LUAD, N=80) and immortalized lung epithelial & fibroblast cell lines (Lung, N=8) from the Human Protein Atlas database. Expression levels are presented as normalized transcript per million (nTPM), b,c Immunofluorescent staining ( b ) and quantification ( c ) of SDHA and SDHD in H1975 cells treated with or without H2/Z14 and C6/Z96 (30 µM) for six hours. Cells were co-stained with primary anti-SDHA and anti-SDHD antibodies, followed by secondary antibodies conjugated with Alexa Fluor 488 or 555. The cells were then counterstained with DAPI and imaged by confocal microscopy. Scale bar = 20 µm. N = 6 replicates. ( d ) Western blot analysis of SDHA in H1975 cells treated with or without H2/Z14 and C6/Z96 (30 µM) for four hours. Band intensity was quantified and is shown below the images. β-Actin was used as a loading control. The images were representative of data from two independent experiments. Data are mean ± s.e.m. and were analyzed with Welch’s t-test ( a , c ). **, p <0.01; ***, p <0.001; ns, not significant

Journal: Cancer Cell International

Article Title: Efficient identification of new small molecules targeting succinate dehydrogenase in non-small cell lung cancer

doi: 10.1186/s12935-025-04002-7

Figure Lengend Snippet: H2/Z14 and C6/Z96 modulate SDH subunit protein abundance.( a ) Normalized expression of SDHA , SDHB , SDHC , and SDHD across human lung adenocarcinoma (LUAD, N=80) and immortalized lung epithelial & fibroblast cell lines (Lung, N=8) from the Human Protein Atlas database. Expression levels are presented as normalized transcript per million (nTPM), b,c Immunofluorescent staining ( b ) and quantification ( c ) of SDHA and SDHD in H1975 cells treated with or without H2/Z14 and C6/Z96 (30 µM) for six hours. Cells were co-stained with primary anti-SDHA and anti-SDHD antibodies, followed by secondary antibodies conjugated with Alexa Fluor 488 or 555. The cells were then counterstained with DAPI and imaged by confocal microscopy. Scale bar = 20 µm. N = 6 replicates. ( d ) Western blot analysis of SDHA in H1975 cells treated with or without H2/Z14 and C6/Z96 (30 µM) for four hours. Band intensity was quantified and is shown below the images. β-Actin was used as a loading control. The images were representative of data from two independent experiments. Data are mean ± s.e.m. and were analyzed with Welch’s t-test ( a , c ). **, p <0.01; ***, p <0.001; ns, not significant

Article Snippet: Fig. 4 H2/Z14 and C6/Z96 modulate SDH subunit protein abundance. ( a ) Normalized expression of SDHA , SDHB , SDHC , and SDHD across human lung adenocarcinoma (LUAD, N=80) and immortalized lung epithelial & fibroblast cell lines (Lung, N=8) from the Human Protein Atlas database.

Techniques: Quantitative Proteomics, Expressing, Staining, Confocal Microscopy, Western Blot, Control