化学
表皮生长因子受体
奥西默替尼
表皮生长因子受体抑制剂
泛素连接酶
酪氨酸激酶
癌症研究
突变体
连接器
T790米
激酶
受体酪氨酸激酶
细胞生长
药理学
肺癌
表皮生长因子
酪氨酸激酶抑制剂
细胞
DNA连接酶
细胞培养
癌症
癌细胞
受体
吉非替尼
信号转导
生长因子受体
流出
埃罗替尼
配体(生物化学)
生物化学
磷酸化
酪氨酸
蛋白酪氨酸激酶
突变
结构-活动关系
作者
Qinyang He,Yan Cheng,Qing Zhang,Huaijiang Xiang,Ningning Fan,Xiuli Yang,Jiaxin Tao,Chunting Qi,李云霞,Siqi Zhou,Mei‐Chun Cai,Pengfei Ma,Mengyang Fan,Hongbin Ji,Yaoyang Zhang,Yujie Fu,Guanglei Zhuang,Li Tan
标识
DOI:10.1021/acs.jmedchem.6c01760
摘要
Abstract Epidermal growth factor receptor (EGFR) mutant-driven non-small cell lung cancer (NSCLC) frequently develops acquired resistance to third-generation tyrosine kinase inhibitors (TKIs), particularly through the EGFR C797S mutation. Existing EGFR-targeting proteolysis-targeting chimeras (PROTACs) remain limited by unfavorable pharmacokinetics and suboptimal selectivity inherited from their parent TKIs. To address these limitations, we developed HQY1480, a next-generation PROTAC derived from the macrocyclic fourth-generation EGFR inhibitor BI-4020. Systematic linker and E3 ligase ligand optimization enabled potent and selective degradation of multiple clinically relevant EGFR mutants with single-digit nanomolar DC50 values. HQY1480 exhibited favorable pharmacokinetics, stronger suppression of oncogenic signaling than BI-4020, and no detectable off-target degradation in proteomic profiling. In xenograft models, HQY1480 outperformed BI-4020, overcame osimertinib resistance, and effectively inhibited tumor growth at low doses, while inducing robust EGFR degradation in patient-derived xenografts. These findings establish HQY1480 as an effective and well-tolerated lead PROTAC for EGFR-mutant NSCLC with acquired resistance to third-generation TKIs.
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