Abstract
Inhibitors targeting mutant EGFR remain a persistent need in combating drug resistance in non-small cell lung cancer. To better understand the molecular factors involved in targeting T790M and C797S mutations, we determined X-ray cocrystal structures of fourth-generation inhibitors BI-8128 and BI-4732. Analysis from molecular dynamics and thermodynamic integration calculations correlated with biochemical and cellular measurements indicate that BI-8128 binds the double T790M/C797S more strongly than the single mutations individually. This observation showcases strengths in the design of these fourth-generation EGFR inhibitors as profile criteria require drugs to inhibit an array of oncogenic and drug resistance mutations.
| Original language | English |
|---|---|
| Pages (from-to) | 531-537 |
| Number of pages | 7 |
| Journal | ACS Medicinal Chemistry Letters |
| Volume | 17 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 12 2026 |
Keywords
- EGFR
- crystallography
- kinase inhibitors
- molecular dynamics
- non-small cell lung cancer
- structural biology
- targeted therapy
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