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Discovery of [1,2,4]triazolo[1,5-a]pyrimidine-Imatinib Hybrids With Selective Cytotoxic Activity: A Mechanistically Divergent Series From Direct BCR-ABL1 Inhibition.

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ChemMedChem 📖 저널 OA 31.1% 2024: 1/3 OA 2025: 4/12 OA 2026: 9/29 OA 2024~2026 2026 Vol.21(8) p. e202501100 OA Chronic Myeloid Leukemia Treatments
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PubMed DOI PMC OpenAlex 마지막 보강 2026-04-29
OpenAlex 토픽 · Chronic Myeloid Leukemia Treatments Synthesis and biological activity Click Chemistry and Applications

Moura SCB, de Oliveira AP, Neto JMR, Dantas RF, Silva-Jr FP, Pimentel LC

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Chronic myeloid leukemia treatment faces the challenge of resistance to BCR-ABL1 tyrosine kinase inhibitors.

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↓ .bib ↓ .ris
APA Stefany Castro Bazan Moura, Andressa Paula de Oliveira, et al. (2026). Discovery of [1,2,4]triazolo[1,5-a]pyrimidine-Imatinib Hybrids With Selective Cytotoxic Activity: A Mechanistically Divergent Series From Direct BCR-ABL1 Inhibition.. ChemMedChem, 21(8), e202501100. https://doi.org/10.1002/cmdc.202501100
MLA Stefany Castro Bazan Moura, et al.. "Discovery of [1,2,4]triazolo[1,5-a]pyrimidine-Imatinib Hybrids With Selective Cytotoxic Activity: A Mechanistically Divergent Series From Direct BCR-ABL1 Inhibition.." ChemMedChem, vol. 21, no. 8, 2026, pp. e202501100.
PMID 42001524 ↗

Abstract

Chronic myeloid leukemia treatment faces the challenge of resistance to BCR-ABL1 tyrosine kinase inhibitors. To address this, we rationally designed six new imatinib-derived compounds 2(a-f) by replacing the quinoline moiety with a [1,2,4]triazolo[1,5-a]pyrimidine scaffold via classical bioisosterism. The compounds were efficiently synthesized and characterized. Biological evaluation revealed that compound 2a exhibited cytotoxic activity in BCR-ABL1-positive K562 cells (47% viability inhibition at 10 µM, IC = 9.7 µM). However, enzymatic assays demonstrated that 2a does not directly inhibit the wild-type ABL1 kinase, unlike IMT. This finding, coupled with its cytotoxicity in nontumorigenic WSS-1 cells, indicates an alternative, off-target mechanism. A clear structure-activity relationship identified the detrimental effect of a -CF substitution. Overall, this work applies bioisosteric replacement to generate a new chemotype and uncovers a mechanistically divergent lead. The distinct, ABL1-independent mechanism of compound 2a establishes a solid foundation for future optimization and highlights its potential as a starting point for developing novel antimyeloproliferative agents with a different therapeutic profile.

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