Salithion

(S)-dioxabenzofos (1.0-144 μM; 24 h) more potently inhibits intracellular AChE activity in SH-SY5Y human neuroblastoma cells than (R)-dioxabenzofos (1.0-144 μM; 24 h), with IC₅₀ values of 5.28 μM and 17.2 μM, respectively, after 24 h of exposure^[1].
(S)-dioxabenzofos (2.5-22.5 μM) exhibits higher bioaffinity for purified AChE than (R)-dioxabenzofos (2.5-22.5 μM), with Stern-Volmer constants of 5.691×10⁴ M^-1 and 1.947×10⁴ M^-1, respectively, and causes greater quenching of AChE intrinsic Trp fluorescence^[1].
(S)-dioxabenzofos forms more stable and numerous noncovalent bonds, including stronger hydrogen bonds, with key active-site residues of AChE than (R)-dioxabenzofos, resulting in a higher calculated bioaffinity (5.012×10⁴ M^-1 vs. 1.905×10⁴ M^-1)^[1].
(S)-dioxabenzofos (200,000 ps) forms more stable, high-affinity complexes with AChE than (R)-dioxabenzofos (200,000 ps) during dynamic simulation, with a lower (more favorable) average binding free energy of -23.55 kcal mol⁻¹ compared to -15.43 kcal mol⁻¹ for (R)-dioxabenzofos^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.