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