Application of reverse molecular docking for the identification of protein targets of S-ethylthiosulphanilate involved in biosurfactant biosynthesis

Aim. The study is focused on determining the effect of the ligand S-ethylthiosulfanylate on protein targets involved in the synthesis of biosurfactants and evaluating their potential interaction. Materials and Methods. A reverse docking approach was employed to investigate the interaction of a single ligand with 8 protein targets. Molecular docking was performed using AutoDock Vina with the Vina scoring function. The preparation of the ligand and protein targets was carried out using AutoDockTools from the MGLTools package. Visualization of the results was accomplished using ChimeraX and BIOVA Discovery Studio. Results. Docking the ligand with 8 protein targets enabled the identification of three promising targets — 3RKY, 2B4Q, and 8IK2 — with affinities lower than –5.5 kcal/mol. Predominantly, hydrogen bonds and hydrophobic interactions were observed, indicating the stability of ligand binding within the active sites of these proteins. Conclusions. The study confirmed the effectiveness of reverse docking for identifying potential protein targets, demonstrating that the ligand can influence biosurfactant biosynthesis through specific interactions with proteins 3RKY, 2B4Q, and 8IK2.