ldn Search Results


trichostatin a  (MedChemExpress)
94
MedChemExpress trichostatin a
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
Trichostatin A, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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embryos  (Selleck Chemicals)
96
Selleck Chemicals embryos
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ldn 193189 2hcl  (Selleck Chemicals)
94
Selleck Chemicals ldn 193189 2hcl
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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compounds ldn 193189  (Tocris)
98
Tocris compounds ldn 193189
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ldn 193189 dihydrochloride  (Tocris)
99
Tocris ldn 193189 dihydrochloride
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ldn 193189  (Aladdin Scientific Corporation)
93
Aladdin Scientific Corporation ldn 193189
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
Ldn 193189, supplied by Aladdin Scientific Corporation, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant proteins ldn 57444 targetmol cat  (Selleck Chemicals)
93
Selleck Chemicals recombinant proteins ldn 57444 targetmol cat
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
Recombinant Proteins Ldn 57444 Targetmol Cat, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ldn 27219  (Tocris)
94
Tocris ldn 27219
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ldn  (Selleck Chemicals)
93
Selleck Chemicals ldn
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
Ldn, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ldn193189  (MedChemExpress)
95
MedChemExpress ldn193189
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ml347  (MedChemExpress)
94
MedChemExpress ml347
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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ldn treated animals  (Biosynth Carbosynth)
86
Biosynth Carbosynth ldn treated animals
Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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Image Search Results


Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and trichostatin A (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1

Journal: Biology Direct

Article Title: LDN-57444 sensitizes hepatocellular carcinoma cells to sorafenib by promoting ferroptosis through histone deacetylase 2 (HDAC2) inhibition

doi: 10.1186/s13062-026-00735-1

Figure Lengend Snippet: Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and trichostatin A (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1

Article Snippet: Erastin (#HY-15763), LDN-57444 (#HY-18637), and trichostatin A (#HY-15144) were purchased from MedChemExpress.

Techniques: Binding Assay, Software, Generated, Thermal Shift Assay