Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran; Student Research Committee, Tabriz University of Medical Sciences, Tabriz, Iran; Department of Medical Physics, School of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran.
Int J Biol Macromol. 2020 Nov 15;163:954-958. doi: 10.1016/j.ijbiomac.2020.07.048. Epub 2020 Jul 10.
Epidermal growth factor receptor (EGFR) plays an important role in cell proliferation at non-small cell lung cancer (NSCLC). Therefore, targeted therapy of cancer via this kind of receptor is highly interested. Small molecule drugs such as erlotinib and gefitinib inhibit EGFR tyrosine kinase and thus suppress cell proliferation. At this paper, erlotinib interaction with EGFR on the cell surface was studied via surface plasmon resonance (SPR) and molecular docking methods. Kinetic parameters indicated that erlotinib affinity toward EGFR was increased through increment of temperature. The thermodynamic analysis showed that van der Waals and hydrogen binding forces play a major role in the interaction of erlotinib with EGFR. Docking results showed that Domain II in EGFR has role in the interaction with erlotinib. Besides, the binding energy for this interaction was -10.7 kcal/mol, which is suitable for binding of erlotinib to Domain II in EGFR.
表皮生长因子受体（EGFR）在非小细胞肺癌（NSCLC）细胞增殖中发挥重要作用。因此，通过这种受体对癌症进行靶向治疗具有很高的兴趣。小分子药物如厄洛替尼和吉非替尼抑制 EGFR 酪氨酸激酶，从而抑制细胞增殖。在本文中，通过表面等离子体共振（SPR）和分子对接方法研究了厄洛替尼与细胞表面 EGFR 的相互作用。动力学参数表明，厄洛替尼与 EGFR 的亲和力通过提高温度而增加。热力学分析表明，范德华力和氢键在厄洛替尼与 EGFR 的相互作用中起主要作用。对接结果表明，EGFR 的结构域 II 在与厄洛替尼的相互作用中起作用。此外，这种相互作用的结合能为-10.7 kcal/mol，适合厄洛替尼与 EGFR 结构域 II 的结合。
