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Montersino, C.

Publications and source records attributed to Montersino, C..

2 recordsLinked to original sources

Identification of AB8939, a novel synthetic microtubule destabilizer and ALDH inhibitor that overcomes multidrug resistance in tumor cells as a drug candidate for the treatment of refractory acute myeloid leukemia

We identified AB8939, a novel small synthetic molecule that exhibits strong and broad antiproliferative activity against a panel of various cancer cell types with IC50 values in the nanomolar range. In vitro investigations showed that AB8939 is a novel microtubule-targeting agent that interacts with the colchicine-binding site of tubulin. AB8939 disrupts the microtubule network, leading to mitotic arrest in G2/M phase and subsequent apoptosis. Importantly, AB8939 overcomes drug resistance mechanisms, including overexpression of efflux transporters such as P-glycoprotein (P-gp) and aberrant expression of {beta}3-tubulin. AB8939 displays high cytotoxicity against blasts from AML patients, including blasts resistant to cytarabine (Ara-C). In vivo, AB8939 shows strong antitumor activity in MOLM-14, an Ara-C-resistant AML model, as evidenced by tumor growth inhibition and substantial increase in mouse survival. Further experiments performed on an AML PDX TG-AML-36 model demonstrated that AB8939 efficiently kills leukemic stem cells (CD34+/CD38-). Reverse proteomic experiments revealed that AB8939 inhibits ALDH1 and ALDH2, enzymes often overexpressed in tumors and tumor stem cells, thereby favoring tumor progression and relapse. AB8939 is a novel dual-targeting drug that acts on both tubulin and ALDH enzymes, with potential activity against various cancer types, especially refractory AML with complex karyotypes such as those displaying MECOM rearrangement and AML with mutations associated with poor prognosis, such as ASXL1 and TP53.

cell biology↗

CRCM5484: A BET- BDII Selective Compound With Differential Anti-Leukemic Drug Potentiation

Differentially screening the Fr-PPIChem chemical library on the BET BRD4-BDII versus -BDI bromodomains led to the discovery of a BDII selective tetrahydropyridothienopyrimidinone (THPTP)-based compound. Structure-activity relationship (SAR) and hit-to-lead approaches allowed us to develop CRCM5484, a potent inhibitor of BET proteins with a preferential and 475-fold selectivity for the second bromodomain of the BRD3 protein (BRD3-BDII) over its first bromodomain (BRD3-BDI). Its very low activity was demonstrated in various cell-based assays, corresponding with recent data describing other selective BDII compounds. However, screening on a drug sensitivity and resistance-profiling platform revealed its ability to modulate the anti-leukemic activity in combination with various FDA-approved and/or in-development drugs in a cell- and context-dependent differential manner. Altogether, the results confirm the originality of the THPTP molecular mode of action in the BD cavity and its potential as starting scaffold for the development of potent and selective bromodomain inhibitors.

cancer biology↗