<![CDATA[Protein tyrosine phosphatase non receptor type 1 (PTPN1) is a key negative regulator of insulin signaling and a validated therapeutic target for antidiabetic drug development. This study investigates the binding potential of three prenylated isoflavanones platyisoflavanone A, sophoraisoflavanone A, and erypogein D against PTP1B using molecular docking. Redocking of the native ligand yielded a low RMSD value (0.2953 Å), confirming the reliability of the docking protocol. All three compounds demonstrated strong predicted affinities and sub‑micromolar Ki values, with platyisoflavanone A showing the highest potency. Interaction analysis revealed that the isoflavanones occupy the catalytic pocket and engage key residues such as Tyr46, Asp48, Phe182, Ile219, and Gln262, supported by extensive hydrophobic contacts from the prenyl substituent. These findings indicate that prenylated isoflavanones possess structural features compatible with PTP1B inhibition and represent promising natural scaffolds for further development of antidiabetic agents.]]>
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