ArticleMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents2026
Integrated 3D-QSAR and cellular profiling of sulfated and hydrophobic aminoglycoside glycans to modulate heparanase activity.
Article in Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Heparanase (HPSE) plays a critical role in tumor progression by degrading heparan sulfate chains in the extracellular matrix and modulating the tumor microenvironment. As a result, it has emerged as a promising therapeutic target. Aminoglycoside-derived sulfated glycan mimetics have shown potential as HPSE inhibitors, but rational optimization is challenged by complex steric and electrostatic interactions. Here, we used three-dimensional quantitative structure-activity relationship (3D-QSAR) modeling to identify key structural features governing HPSE inhibition, providing new predictive structure-activity insights for sulfated aminoglycoside-based HPSE inhibitors. Guided by these insights, we evaluated the lead compound L17 in HPSE-dependent cancer cell lines and observed concentration-dependent inhibition of proliferation, suppression of invasion, and reduction of extracellular HPSE levels. In silico ADMET predictions flagged CYP3A4 as a potential liability, but experimental assays confirmed minimal inhibition, indicating a favorable metabolic profile. This integrated approach provides mechanistic insight into aminoglycoside-based HPSE inhibitors and supports their rational optimization as anticancer therapeutics.
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