Probing conformational dynamics of EGFR mutants via SEIRA spectroscopy: potential implications for tyrosine kinase inhibitor design.
Phys Chem Chem Phys
; 2024 Aug 23.
Article
in 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Phys Chem Chem Phys
Journal subject:
BIOFISICA
/
QUIMICA
Year:
2024
Document type:
Article
Affiliation country:
Italy