Identification of dual inhibitors of ROCK1 and TGFBR1 for overcoming metastasis: an integrated pharmacophore and docking driven CADD strategy

鉴定ROCK1和TGFBR1双重抑制剂以克服转移:一种整合药效团和分子对接驱动的计算机辅助药物设计策略

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Abstract

Rho-associated coiled-coil kinase 1 (ROCK1) and transforming growth factor-beta receptor 1 (TGFBR1) plays crucial roles in epithelial-mesenchymal transition (EMT), cytoskeleton remodeling, cell adhesion, and tumor metastasis. Targeting both ROCK1 and TGFBR1 simultaneously offers a strategic approach to disrupt these pathways, potentially leading to more effective treatments for cancer metastasis. To identify dual inhibitors, a multifaceted computational approach integrating pharmacophore modeling, molecular docking, and molecular dynamics (MD) simulations was employed. Pharmacophore models were derived from the PDB structures of ROCK1 and TGFBR1 and validated based on their ability to discriminate between known active and inactive inhibitors from the ChEMBL database with performance evaluated using Receiver Operating Characteristic Area Under the Curve (ROC AUC) calculations. These validated pharmacophore models were used to virtually screen a diverse set of 1,48,648 compounds, identifying promising candidates for dual inhibition. Top-ranking compounds from the pharmacophore screening were subjected to molecular docking studies to evaluate their binding interactions with ROCK1 and TGFBR1. The most promising candidates, Hit-1, Hit-2, and Hit-3, were further analyzed through 200-ns molecular dynamics simulations to assess their stability and interaction dynamics with the hinge residues of both targets. Among the screened compounds, Hit-2, (4-(1,3-dimethyl-1H-pyrazol-4-yl)-N-[2-(pyridin-3-yloxy)propyl]pyrimidin-2-amine) exhibited the most favourable binding affinity (- 155.801 kJ/mol) for ROCK1 and (- 213.264 kJ/mol) for TGFBR1, structural stability, and interaction profile, suggesting its potential as a dual inhibitor of ROCK1 and TGFBR1. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s40203-025-00414-5.

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