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Probing conformational dynamics of EGFR mutants via SEIRA spectroscopy: potential implications for tyrosine kinase inhibitor design
Physical Chemistry Chemical Physics ( IF 2.9 ) Pub Date : 2024-08-19 , DOI: 10.1039/d4cp02232g Emiliano Laudadio 1 , Federica Piccirilli 2, 3 , Henrick Vondracek 2, 4 , Giovanna Mobbili 5 , Marta S Semrau 2 , Paola Storici 2 , Roberta Galeazzi 5 , Elena Romagnoli 5 , Leonardo Sorci 1 , Andrea Toma 6 , Vincenzo Aglieri 6 , Giovanni Birarda 2 , Cristina Minnelli 5
Physical Chemistry Chemical Physics ( IF 2.9 ) Pub Date : 2024-08-19 , DOI: 10.1039/d4cp02232g Emiliano Laudadio 1 , Federica Piccirilli 2, 3 , Henrick Vondracek 2, 4 , Giovanna Mobbili 5 , Marta S Semrau 2 , Paola Storici 2 , Roberta Galeazzi 5 , Elena Romagnoli 5 , Leonardo Sorci 1 , Andrea Toma 6 , Vincenzo Aglieri 6 , Giovanni Birarda 2 , Cristina Minnelli 5
Affiliation
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Missense mutations in EGFR's catalytic domain alter its function, promoting cancer. SEIRA spectroscopy, supported by MD simulations, reveals structural differences in the compactness and hydration of helical motifs between active and inactive EGFR conformations models. These findings provide novel insights into the biophysical mechanisms driving EGFR activation and drug resistance, offering a robust method for studying emerging EGFR mutations and their structural impacts on TKIs’ efficacy.
中文翻译：
通过 SEIRA 光谱探测 EGFR 突变体的构象动力学：对酪氨酸激酶抑制剂设计的潜在影响
EGFR 催化结构域的错义突变改变其功能，促进癌症。在 MD 模拟的支持下，SEIRA 光谱揭示了活性和非活性 EGFR 构象模型之间螺旋基序的致密性和水合作用的结构差异。这些发现为驱动 EGFR 激活和耐药性的生物物理机制提供了新的见解，为研究新兴 EGFR 突变及其对 TKI 功效的结构影响提供了可靠的方法。
更新日期：2024-08-23
中文翻译：
通过 SEIRA 光谱探测 EGFR 突变体的构象动力学：对酪氨酸激酶抑制剂设计的潜在影响
EGFR 催化结构域的错义突变改变其功能，促进癌症。在 MD 模拟的支持下，SEIRA 光谱揭示了活性和非活性 EGFR 构象模型之间螺旋基序的致密性和水合作用的结构差异。这些发现为驱动 EGFR 激活和耐药性的生物物理机制提供了新的见解，为研究新兴 EGFR 突变及其对 TKI 功效的结构影响提供了可靠的方法。
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