Chemical Research in Chinese Universities ›› 2026, Vol. 42 ›› Issue (5): 1560-1571.doi: 10.1007/s40242-026-6078-0

• Research Articles • Previous Articles     Next Articles

Disease-anchored Network Analysis and Molecular Dynamics Prioritize HSP90AB1 as a Doxorubicin-binding Hub Across Cancers

WANG Wentao1,2, LI Sen1, CAI Yanfei1, CHEN Yun1, ZHU Jingyu1, JIN Jian1   

  1. 1. School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China;
    2. School of Chemical and Material Engineering, Jiangnan University, Wuxi 214122, P. R. China
  • Received:2026-03-26 Accepted:2026-05-18 Online:2026-10-01 Published:2026-09-24
  • Supported by:
    This work was supported by the National Natural Science Foundation of China (No. 21807049) and the Fundamental Research Funds for the Central Universities, China (No. JUSRP51703A).

Abstract: Doxorubicin functions through DNA-centered mechanisms and protein-level interactions; however, the cancer-relevant binding hubs remain inadequately defined. We integrated a previously reported functional protein microarray dataset for doxorubicin, which comprised 363 reproducible binders, alongside GeneCards and GeDiPNet disease-gene resources for breast cancer, non-Hodgkin lymphoma, and lymphoblastic leukemia. The three disease gene sets shared a total of 962 genes and were enriched for pathways related to immune activation, chromosomal organization, DNA damage responses, and cancer/viral infections. Disease-anchored binders were assembled into a STRING network and ranked using four centrality measures from cytoHubba. Seven consensus hubs were retained, with HSP90AB1 ranking first by WeightedMean score (16.18). HSP90AB1 also constituted the core of the complete 363-binder network. Docking experiments positioned doxorubicin within the N-terminal ATP-binding pocket of HSP90AB1, supported by recurrent polar, water-mediated, and aromatic interactions. In 400 ns simulations, doxorubicin remained associated with the binding pocket, exhibited stable ligand radius of gyration (rGyr) (approximately 5.0 Å to 5.3 Å, 1 Å=0.1 nm), had a higher ligand solvent accessible surface area (SASA) than KU3 (135.91 vs. 92.46 Å2), and produced ligand-dependent principal component analysis (PCA) profiles. Trajectory-sampled molecular mechanics/generalized Born surface area (MM/GBSA) analyses favored doxorubicin over KU3 [(-88.83±11.87) vs. (-51.08±3.55) kcal/mol]. These findings emphasize HSP90AB1 as a critical doxorubicin-binding hub relevant to disease.

Key words: Doxorubicin, HSP90AB1, Protein microarray, Disease database, Molecular docking, Molecular dynamics simulation