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Methodology for Multi‐Site Ligand–Protein Docking Identification Developed for the Optimization of Spirostenol Inhibition of β‐Amyloid‐Induced Neurotoxicity

Spirostenol steroids have been found to inhibit β‐amyloid‐induced neurotoxicity. We have evaluated in parallel experimental and molecular‐modeling studies the relative effectiveness of 17 (22R)‐hydroxycholesterol derivatives in binding to the target peptide. Our results support the previous evidence that β‐amyloid offers multiple docking sites for these steroids. Molecular modeling allowed for the correlation of spirostenol candidate structural differences with a choice of proposed active sites. A multi‐site identification technique based on a Site‐Identifier Matrix (SIM) was developed that clearly showed the uniqueness of our lead (maximum neurotoxicity inhibition) candidate SP233, with a nearly equal docking affinity for two sites.