Probing conformational dynamics of EGFR mutants via SEIRA spectroscopy: potential implications for tyrosine kinase inhibitor design

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.

Autori

Emiliano Laudadio, Federica Piccirilli, Henrick Vondracek, Giovanna Mobbili, Marta Stefania Semrau, Paola Storici, Roberta Galeazzi, Elena Romagnoli, Leonardo Sorci, Andrea Toma, Vincenzo Aglieri, Giovanni Birarda, Cristina Minnelli

Rivista

Physical Chemistry Chemical Physics (PCCP)

Data di pubblicazione

19/08/2024

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