Computational analysis reveals improved binding affinity and reduced toxicity of novel FGFR1 inhibitors for targeted drug discovery.
Aberrant activation of fibroblast growth factor receptor 1 (FGFR1) drives tumor progression in multiple cancer types, yet existing FGFR1 inhibitors suffer from suboptimal target selectivity and dose-limiting toxicities. This study describes an integrated computational approach for the identification of novel FGFR1 inhibitors. We established a computational pipeline incorporating ligand-based pharmacophore modeling, multi-tiered virtual screening with hierarchical docking (HTVS/SP/XP), and MM-GBSA binding energy calculations to evaluate interactions within the FGFR1 kinase domain. From an initial library of 9019 anticancer compounds, three hit compounds exhibited superior FGFR1 binding affinity compared to the reference ligand 4UT801. Scaffold hopping was performed to generate 5355 structural derivatives, among which candidate compounds 20357a–20357c showed improved bioavailability and reduced toxicity as predicted by absorption, distribution, metabolism, excretion, and toxicity (ADMET) profiling. Molecular dynamics (MD) simulations validated stable binding modes and favorable interaction energies for these candidates. Collectively, our study identifies structurally novel FGFR1 inhibitors with optimized pharmacodynamic and safety profiles, thereby advancing targeted anticancer drug discovery.
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Ji et al. (2025) studied this question.
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