Binding and Stability of Magnoflorine with Steroid Sulfatase

Background: Steroid sulfatase (STS) plays a critical role in estrogen biosynthesis and may represent an important therapeutic target in estrogen receptor–positive breast cancer. This study investigated the potential of bioactive alkaloid Magnoflorine as STS inhibitor using computational approaches. Methods: Molecular docking and dynamics simulations were employed to evaluate binding affinity, stability, and dynamic behavior of Magnoflorine–STS complex. Key parameters, including atomic deviations, residual fluctuations, free energy calculations, and following pharmacokinetics profiles, were analyzed. Results: Magnoflorine demonstrated a favorable binding affinity (−8.1 kcal/mol) and formed stable interactions with STS. Molecular dynamics analyses revealed stable complex formation with lower structural fluctuations compared to Tranilast. Free energy and conformational analyses supported sustained binding stability with an acceptable pharmacokinetic and toxicity profile. Conclusion: Magnoflorine may act as a promising STS regulator with potential relevance for estrogen-dependent breast cancer therapy and warrants experimental validation.