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Updated: Jun 15, 2025

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
Published on: May 20, 2020
Probing conformational dynamics of EGFR mutants via SEIRA spectroscopy: potential implications for tyrosine kinase
Emiliano Laudadio1, Federica Piccirilli2,3, Henrick Vondracek2,4
1Department of Science and Engineering of Matter, Environment and Urban Planning, Marche Polytechnic University, 60131, Ancona, Italy.
Abstract:
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.
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