Elucidating the isorhamnetin-3-O-glucoside-iNOS interaction via molecular dynamics and Hirshfeld surface analyses.

ABSTRACT: Inducible nitric oxide synthase (iNOS) remains a demanding metallo-enzyme target because the catalytic heme shapes both geometry and electrostatics at the binding site. We evaluated the dietary flavonol glycoside isorhamnetin-3-O-glucoside (I3OG) against mouse (3E6T) and human (3E7G) iNOS oxygenase domains using a heme-aware, auditably validated docking workflow. we centered the docking grids at the crystallographic Fe position and validated the protocol by re-docking the native co-crystallized inhibitors (3E6T: AR-C118901/1A2; 3E7G: AR-C95791/AT2), reproducing the crystal poses with heavy-atom RMSD = 1.093 Å and 0.327 Å, respectively (≤ 2.0 Å criterion). Explicit-solvent 100-ns MD confirmed stable complexes for both systems; 3E6T showed tighter ligand RMSD, lower pocket Cα-RMSF, and a mor

SUBMITTER: Khibech O 

PROVIDER: S-EPMC12716702 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature