非小细胞肺癌 (NSCLC) 患者通常受益于吉非替尼等 EGFR 抑制剂。然而，耐药性仍然是治疗中的重大挑战。 1,2,3-三唑是一种氮基化合物，其独特的性质因其多功能的结构属性和多种生物效应（包括抗癌特性）而有望成为潜在的解决方案。我们的合成过程涉及胡伊斯根环加成化学方法，该方法产生了多种埃克替尼衍生物。我们评估了这些衍生物针对各种癌细胞系的抗癌能力，特别关注表现出耐药性的 NSCLC 细胞。此外，我们使用表面等离子共振 (SPR) 实验研究了所选化合物（包括 3l）对野生型 EGFR 的结合亲和力。值得注意的是，埃克替尼衍生物（例如衍生物 3l）对不同的癌细胞系（包括对传统的耐药细胞系）表现出显着的功效。疗法。化合物 3l 对耐药细胞表现出有效的活性，IC50 值低于 10 μM。 SPR 实验表明，与埃克替尼相比，3l 对野生型 EGFR 的亲和力增强。我们的研究结果表明，3l 是 EGFR 蛋白酪氨酸激酶 (EGFR-PTK) 的强效拮抗剂。埃克替尼衍生物 3l 具有 1,2,3-三唑环，对耐药 NSCLC 细胞具有有效的抗癌作用。它增强了对 EGFR 的结合亲和力，并对 EGFR-RAS-RAF-MAPK 通路位置 3l 进行调节，成为未来抗癌药物开发的有希望的候选药物。版权所有 © Bentham Science Publishers；如有任何疑问，请发送电子邮件至 epub@benthamscience.net。

Non-small cell lung cancer (NSCLC) patients often benefit from EGFR inhibitors like gefitinib. However, drug resistance remains a significant challenge in treatment. The unique properties of 1,2,3-triazole, a nitrogen-based compound, hold promise as potential solutions due to its versatile structural attributes and diverse biological effects, including anticancer properties.Our synthesis process involved the huisgen cycloaddition chemical method, which generated diverse icotinib derivatives. We evaluated the anticancer capabilities of these derivatives against various cancer cell lines, with a specific focus on NSCLC cells that exhibit drug resistance. Additionally, we investigated the binding affinity of selected compounds, including 3l, towards wild-type EGFR using surface plasmon resonance (SPR) experiments.Notably, icotinib derivatives such as derivative 3l demonstrated significant efficacy against different cancer cell lines, including those resistant to conventional therapies. Compound 3l exhibited potent activity with IC50 values below 10 μM against drug-resistant cells. SPR experiments revealed that 3l exhibited enhanced affinity towards wild-type EGFR compared to icotinib. Our research findings suggest that 3l acts as a compelling antagonist for the protein tyrosine kinase of EGFR (EGFR-PTK).Icotinib derivative 3l, featuring a 1,2,3-triazole ring, demonstrates potent anticancer effects against drug-resistant NSCLC cells. Its enhanced binding affinity to EGFR and modulation of the EGFR-RAS-RAF-MAPK pathway position 3l as a promising candidate for the future development of anticancer drugs.Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.