1869033-49-7
Chemical Structure
AM9928
- CAS No.: 1869033-49-7
- Formula:C24H20N4O2
- Molecular Weight:396.44
InChIKey: FXNXCSUZLHXTGH-UHFFFAOYSA-N
SMILES: N#CC1=CC(OC(N2CCN(C3C4=C(C5=C3C=CC=C5)C=CC=C4)CC2)=O)=NC=C1
Biological Activity: AM9928 is a monoacylglycerol lipase (MAGL) inhibitor with IC50 and Ki values of 8.9 nM and 7.3 nM, respectively. AM9928 blocks the adhesion and migration of triple-negative breast cancer (TNBC) cells, and inhibits the secretion of IL-6, IL-8 and VEGF-A by TNBC cells. AM9928 suppresses the activation of human brain microvascular endothelial cells (HBMECs) induced by TNBC-derived exosomes, and reduces the secretion of IL-8 and VEGF-A by HBMECs. AM9928 attenuates changes in blood-brain barrier permeability, inhibits tumor growth in the mammary fat pad, and reduces brain colonization of TNBC. AM9928 can be used in studies related to triple-negative breast cancer[1][2][3].
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AM9928 | AM9928 is a monoacylglycerol lipase (MAGL) inhibitor with IC50 and Ki values of 8.9 nM and 7.3 nM, respectively. AM9928 blocks the adhesion and migration of triple-negative breast cancer (TNBC) cells, and inhibits the secretion of IL-6, IL-8 and VEGF-A by TNBC cells. AM9928 suppresses the activation of human brain microvascular endothelial cells (HBMECs) induced by TNBC-derived exosomes, and reduces the secretion of IL-8 and VEGF-A by HBMECs. AM9928 attenuates changes in blood-brain barrier permeability, inhibits tumor growth in the mammary fat pad, and reduces brain colonization of TNBC. AM9928 can be used in studies related to triple-negative breast cancer. | |||||||||||||||||||||
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References
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[1]. Avraham S, et al. Targeting Monoacylglycerol Lipase in Triple-Negative Breast Cancer Reduced Tumor-Associated Inflammation and Decreased Colonization in the Brain. Authorea Preprints. 2024 Jan 31.
- [2]. Zhang Y, et al. Drug Treatment Direction Based on the Molecular Mechanism of Breast Cancer Brain Metastasis. Pharmaceuticals (Basel). 2025;18(2):262. Published 2025 Feb 16. [Content Brief]
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[3]. Nasr ML. Biochemical and biophysical characterization of human monoacylglycerol lipase in solution and in the presence of nanodisc membrane models.
