Aim: This study aims to investigate the binding affinity and interaction mechanism of Yakuchinone B, a bioactive diarylheptanoid, against key inflammatory targets, including Cyclooxygenase-1 (COX-1), Cyclooxygenase-2 (COX-2), 5-Lipoxygenase (LOX-5), and Thromboxane A2 (TXA-2), using a molecular docking approach. Methodology: A molecular docking study was performed using Schrodinger software. The 3D structure of Yakuchinone B was optimized, and the crystallographic structures of the inflammatory targets were retrieved from the Protein Data Bank (PDB). Docking simulations were executed to evaluate binding energies, interaction profiles, and amino acid residues involved in target inhibition. Comparative analysis with standard anti-inflammatory drugs was conducted to assess Yakuchinone B__ampersandsignrsquo;s relative efficacy. Results: Yakuchinone B exhibited significant binding affinities with all four inflammatory targets, with the highest docking score observed against COX-2, indicating potential selectivity. The analysis revealed critical hydrogen bonding, hydrophobic interactions, and __ampersandsignpi;__ampersandsignndash;__ampersandsignpi; stacking with essential amino acid residues of the active sites. The binding energies of Yakuchinone B were comparable to or better than those of standard anti-inflammatory agents, highlighting its competitive potential as a multi-target inhibitor. Conclusion: The molecular docking analysis demonstrates Yakuchinone B__ampersandsignrsquo;s strong binding affinity and multi-target inhibitory potential against COX-1, COX-2, LOX-5, and TXA-2. These findings support further in vitro and in vivo investigations to establish its role as a promising anti-inflammatory agent, thereby promoting its development as a novel therapeutic candidate.