Probing conformational dynamics of EGFR mutants via SEIRA spectroscopy: potential implications for tyrosine kinase inhibitor design.
Phys Chem Chem Phys
; 26(35): 22853-22857, 2024 Sep 11.
Article
en En
| MEDLINE
| ID: mdl-39177248
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.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Inhibidores de Proteínas Quinasas
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Simulación de Dinámica Molecular
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Receptores ErbB
Límite:
Humans
Idioma:
En
Revista:
PCCP. Phys. chem. chem. phys. (Print)
/
PCCP. Physical chemistry chemical physics (Print)
/
Phys Chem Chem Phys
Asunto de la revista:
BIOFISICA
/
QUIMICA
Año:
2024
Tipo del documento:
Article
País de afiliación:
Italia