Chemical Research in Chinese Universities ›› 2026, Vol. 42 ›› Issue (5): 1591-1595.doi: 10.1007/s40242-026-6100-6

• Research Articles • Previous Articles     Next Articles

Rational Design and Synthesis of Novel Allosteric Hsp70 Inhibitors via a Scaffold-hopping Strategy

WANG Siyao1, WANG Zheming1, SHENG Zhijue2, ZHANG Hong3, SONG Ting3, SONG Yang4, WANG Ziqian3, ZHANG Zhichao3   

  1. 1. Central Hospital of Dalian University of Technology (Dalian Central Hospital), School of Chemistry, Dalian University of Technology, Dalian 116024, P. R. China;
    2. School of Pharmaceutical Sciences, Jinlin University, Changchun 130021, P. R. China;
    3. Central Hospital of Dalian University of Technology (Dalian Central Hospital), Faculty of Medicine, Dalian University of Technology, Dalian 116024, P. R. China;
    4. Department of Hematology, Central Hospital of Dalian University of Technology (Dalian Central Hospital), Dalian University of Technology, Dalian 116024, P. R. China
  • Received:2026-04-25 Accepted:2026-05-08 Online:2026-10-01 Published:2026-09-24
  • Supported by:
    This work was supported by the National Natural Science Foundation of China (Nos. 82500215, 82270186, and 82273778), the Fundamental Research Funds for the Central Universities, China (No. DUT24YG153), and the Dalian City Life and Health Guidance Plan Project, China (No. 2024ZDJH01PT012).

Abstract: Heat shock protein 70 (Hsp70) family proteins play a critical role in chronic myeloid leukemia (CML) cells’ survival. Based on the Hsp70 inhibitor JG-98, we developed a new class of inhibitors via a scaffold-hopping strategy. A “privileged structure” in medicinal chemistry replaces the benzothiazole group of JG-98. Through optimization, structure-activity relationship (SAR) analysis, and molecular docking, we gained compounds Q3 and Q4, which achieved the same level of ATPase activity inhibition of mitochondrial Hsp70, GRP75, as JG-98. They exhibit a lower molecular weight than JG-98. Q3 and Q4 maintain a comparable cytotoxic activity with JG-98 against the CML cell line, K562 cells.

Key words: Heat shock protein 70 (Hsp70) family protein, Antitumor, Structure-activity relationship