ArticleScientific reports2026
Computational characterization of GRP78 binding sites on mitochondrial GPX4: implications for targeting ferroptosis in triple-negative breast cancer.
Article in Scientific reports, 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
About 20% of breast cancer cases are triple-negative breast cancer (TNBC), a highly aggressive subtype with limited therapeutic options. Emerging evidence suggests that ferroptosis - a form of regulated cell death - and stress-response pathways play critical roles in TNBC progression. We investigated the interaction between glucose-regulated protein 78 (GRP78), a central stress-response chaperone, and mitochondrial glutathione peroxidase 4 (mGPX4), a key regulator of ferroptosis resistance. Using a combined computational approach - including protein-protein docking, molecular dynamics (MD) simulations, and MM/GBSA free-energy calculations - we identified stable complexes between GRP78's SBDβ domain and several regions of mGPX4. Docking with PRODIGY revealed binding affinities ranging from - 7.7 ± 0.5 to - 10.5 ± 0.6 kcal/mol, surpassing that of Pep42 (-6.9 ± 0.1 kcal/mol), with region III (the mitochondrial import sequence) showing the strongest binding (-10.5 ± 0.6 kcal/mol). HADDOCK scoring further highlighted region II as particularly favorable (-72.0 ± 5.4). After 100 ns of MD, MM/GBSA analysis estimated binding free energies from - 45.20 to - 86.39 kcal/mol, with the region-II complex exhibiting the highest affinity (-86.4 kcal/mol), driven predominantly by electrostatic and van der Waals interactions. This interaction could serve as a promising therapeutic target to undermine cancer cell survival by sensitizing TNBC cells to ferroptosis-inducing strategies.
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