AI Article Synopsis
- The epidermal growth factor receptor (EGFR) is crucial in cancer development, and targeting its mutant forms has led to three generations of approved inhibitors.
- The quinazoline structure is particularly effective for creating new EGFR inhibitors because it binds well to the active site of the EGFR kinase.
- This review discusses the structural changes that enhance the effectiveness against common and resistant EGFR mutants, and highlights new quinazoline derivatives being developed as potential inhibitors.
Article Abstract
The epidermal growth factor receptor (EGFR) plays a critical role in the tumorigenesis of various forms of cancer. Targeting the mutant forms of EGFR has been identified as an attractive therapeutic approach and led to the approval of three generations of inhibitors. The quinazoline core has emerged as a favorable scaffold for the development of novel EGFR inhibitors due to increased affinity for the active site of EGFR kinase. Currently, there are five first-generation (gefitinib, erlotinib, lapatinib, vandetanib, and icotinib) and two second-generation (afatinib and dacomitinib) quinazoline-based EGFR inhibitors approved for the treatment of various types of cancers. The aim of this review is to outline the structural modulations favorable for the inhibitory activity toward both common mutant (del19 and L858R) and resistance-conferring mutant (T790M and C797S) EGFR forms, and provide an overview of the newly synthesized quinazoline derivatives as potentially competitive, covalent or allosteric inhibitors of EGFR.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10141396 | PMC |
| http://dx.doi.org/10.3390/ph16040534 | DOI Listing |
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