ldn Search Results


compounds ldn 193189  (Tocris)
98
Tocris compounds ldn 193189
Compounds Ldn 193189, supplied by Tocris, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/compounds ldn 193189/product/Tocris
Average 98 stars, based on 1 article reviews
compounds ldn 193189 - by Bioz Stars, 2026-04
98/100 stars
  Buy from Supplier
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
https://www.bioz.com/result/trichostatin a/product/MedChemExpress
Average 94 stars, based on 1 article reviews
trichostatin a - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier
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
Ldn 193189 Dihydrochloride, supplied by Tocris, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ldn 193189 dihydrochloride/product/Tocris
Average 99 stars, based on 1 article reviews
ldn 193189 dihydrochloride - by Bioz Stars, 2026-04
99/100 stars
  Buy from Supplier
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
Ldn 27219, supplied by Tocris, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ldn 27219/product/Tocris
Average 94 stars, based on 1 article reviews
ldn 27219 - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier
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
Ldn193189, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ldn193189/product/MedChemExpress
Average 95 stars, based on 1 article reviews
ldn193189 - by Bioz Stars, 2026-04
95/100 stars
  Buy from Supplier
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
Ml347, 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
https://www.bioz.com/result/ml347/product/MedChemExpress
Average 94 stars, based on 1 article reviews
ml347 - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier
quercetin 3 r  (ChromaDex)
91
ChromaDex quercetin 3 r
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
Quercetin 3 R, supplied by ChromaDex, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/quercetin 3 r/product/ChromaDex
Average 91 stars, based on 1 article reviews
quercetin 3 r - by Bioz Stars, 2026-04
91/100 stars
  Buy from Supplier
dihydromyricetin chromadex irvine ca  (ChromaDex)
86
ChromaDex dihydromyricetin chromadex irvine ca
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
Dihydromyricetin Chromadex Irvine Ca, supplied by ChromaDex, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/dihydromyricetin chromadex irvine ca/product/ChromaDex
Average 86 stars, based on 1 article reviews
dihydromyricetin chromadex irvine ca - by Bioz Stars, 2026-04
86/100 stars
  Buy from Supplier
sb431542  (Selleck Chemicals)
96
Selleck Chemicals sb431542
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
Sb431542, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sb431542/product/Selleck Chemicals
Average 96 stars, based on 1 article reviews
sb431542 - by Bioz Stars, 2026-04
96/100 stars
  Buy from Supplier
ldn 57444 ldn  (Selleck Chemicals)
93
Selleck Chemicals ldn 57444 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 57444 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
https://www.bioz.com/result/ldn 57444 ldn/product/Selleck Chemicals
Average 93 stars, based on 1 article reviews
ldn 57444 ldn - by Bioz Stars, 2026-04
93/100 stars
  Buy from Supplier
ldn 193189  (Miltenyi Biotec)
94
Miltenyi Biotec 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 Miltenyi Biotec, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ldn 193189/product/Miltenyi Biotec
Average 94 stars, based on 1 article reviews
ldn 193189 - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier
stemmacs ldn 193189  (Miltenyi Biotec)
94
Miltenyi Biotec stemmacs 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
Stemmacs Ldn 193189, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/stemmacs ldn 193189/product/Miltenyi Biotec
Average 94 stars, based on 1 article reviews
stemmacs ldn 193189 - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier

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