bims-midomi Biomed News
on MDM2 and mitochondria
Issue of 2025–09–07
six papers selected by
Gavin McStay, Liverpool John Moores University



  1. Arch Pharm (Weinheim). 2025 Sep;358(9): e70085
      Inhibiting the p53-MDM2 interaction restores the function of the tumour suppressor protein, p53, and offers a promising avenue for anticancer therapies. Herein, a novel series of pyrazoline-derived compounds was developed and synthesised to serve as potential inhibitors of the p53-MDM2 interaction. Scaffold hopping was adopted via replacing the cis-imidazoline core of Nutlin-2 with a pyrazoline core, and molecular docking confirmed the binding orientation of the designed compounds at the p53-MDM2 interaction site. The antiproliferative activities of these compounds were evaluated against the NCI60 cell lines, where compounds 6c, 6d and 9d displayed the highest inhibitory activities. Subsequently, compound 6d was selected for the five-doses NCI60 cell panel assay to afford a mean GI50 value of 8.39 μM. Moreover, 6d significantly reduced MDM2 expression and elevated the expression of p53 in an ELISA-based assay, yielding a biochemical IC50 value of 13.8 μM against MDM2, which was confirmed by Western blot as well. Cytotoxicity study confirmed the selectivity of 6d towards cancerous cell lines over normal cell lines. Additionally, X-ray crystallography was used to check the stereochemistry of compound 6d. These newly identified MDM2 inhibitors represent promising candidates for the development of novel targeted anticancer agents.
    Keywords:  MDM2 inhibition; X‐ray diffraction; anticancer activity; p53‐MDM2 interaction; synthesis; wild‐type p53
    DOI:  https://doi.org/10.1002/ardp.70085
  2. Mol Ther Oncol. 2025 Sep 18. 33(3): 201029
      Novel pharmacological strategies capable of inhibiting pro-oncogenic MDM2 beyond its p53-dependent functions represent increasingly attractive therapeutic strategies to treat solid and hematological cancers that are dependent upon MDM2/MDMX, regardless of TP53 mutational status. Utilizing a novel first-in-class cell-penetrating peptide disruptor of MDM2 homo- and heterodimerization (DRx-098D), we demonstrate the anti-proliferative potential of blocking MDM2 dimerization against a panel of human cancer cell lines that are TP53 wild type, mutant, or null. DRx-098D elicits its anti-cancer activity via a differentiated mechanism vs. idasanutlin (a phase 3 clinical candidate MDM2-p53 small-molecule inhibitor), inducing significantly superior growth inhibition against TP53 null HCT116 cells. Our preliminary data highlight, for the first time, the potential therapeutic utility of exploiting both MDM2 homo- and heterodimerization in TP53 wild-type and mutant cancers with an MDM2-derived disruptor peptide.
    Keywords:  MDM2; MDMX; MT: Regular Issue; TP53 mutant cancer; dimerization; disruptor peptide
    DOI:  https://doi.org/10.1016/j.omton.2025.201029
  3. Pathol Res Pract. 2025 Oct;pii: S0344-0338(25)00379-6. [Epub ahead of print]274 156186
       OBJECTIVE: Pancreatic cancer is one of the most aggressive malignant tumors in humans, with poor prognosis. The acetylase tumor inhibitor (Pracinostat) has been shown to suppress the growth of various tumors. This study aimed to investigate the effects of Pracinostat on the pancreatic cancer cell line BxPC3 and to explore the underlying molecular mechanisms through both in vivo and in vitro experiments.
    METHODS: BxPC3 cells were treated with Pracinostat, and cell viability was assessed by CCK-8 assay; the differentially expressed miRNAs in cells before and after pracinostat treatment were screened by high-throughput sequencing, and miR-381-3p was selected as the target gene; the targeting relationship between miR-381-3p and MDM2 was verified by double luciferase reporter gene; the relationship between miR-381-3p, MDM2 and P53 signaling pathways was verified by immunoprecipitation, Western blot and other experiments. Pancreatic tumor models were established in BALB/c nude mice to study the role of pracinostat in vivo.
    RESULTS: Pracinostat upregulated the expression of miR-381-3p and p53, while downregulating MDM2 expression. It also inhibited the proliferation and migration of pancreatic cancer cells and promoted apoptosis. Treatment with a miR-381-3p inhibitor reversed the effects of Pracinostat. In addition, MDM2 was found to promote the ubiquitination and degradation of p53 via the ubiquitin-proteasome pathway. In vivo experiments confirmed that Pracinostat inhibited tumor growth in nude mice.
    CONCLUSION: pracinostat activates the p53 signaling pathway by targeting the miR-381-3p/MDM2 axis, thereby inhibiting the proliferation of pancreatic cancer cells. These findings provide novel insights and potential therapeutic strategies for pancreatic cancer, and may also provide a reference for the treatment of other malignancies.
    Keywords:  Degradation of p53 ubiquitination; MDM2; MiR-381–3p; Pancreatic cancer; Pracinostat
    DOI:  https://doi.org/10.1016/j.prp.2025.156186
  4. Cell Death Discov. 2025 Aug 29. 11(1): 416
      The lymphotoxin β receptor (LTβR), a key activator of non-canonical NF-κB signaling, is expressed in various cells, including cancer cells. Although high expression of LTβR has been associated with poor patient prognosis and drug resistance, conflicting evidence suggested that LTβR induces apoptosis. To investigate the functional role of LTβR in tumors, we performed LTβR knockdown in cancer cells. We found that LTβR knockdown induced senescence phenomena such as reduced cell number; increased cell size; increased SA-β-Gal activity; and upregulated p53, MDM2 and p21 expression. Moreover, LTβR knockdown induced p21-mediated senescence in p53 WT cancer cells, but not in p53 mutant cancer cells. The level of p53 is regulated by MDM2 and MDMX; MDMX enhances MDM2 activity but is also subject to MDM2-mediated degradation in the nucleus. We found that the intracellular domain of LTβR bound to MDMX thereby inhibited its nuclear translocation, which in turn reduced MDMX ubiquitination and consequently promoted p53 ubiquitination. Additionally, tumors derived from B16F10LTβR-KO cells in WT mice exhibited significantly reduced growth compared to those derived from B16F10WT cells. These results demonstrate that LTβR regulates p53 protein levels by modulating MDMX stability and localization, resulting in p53-mediated cellular senescence. LTβR regulates p53-mediated senescence by inhibiting MDMX nuclear translocation and degradation. LTβR interacts with MDMX in the cytoplasm, preventing its nuclear translocation and degradation under normal conditions (dotted arrows). When LTβR is depleted, MDMX is translocated into the nucleus by MDM2, and undergoes degradation (solid arrows). This reduces p53 degradation and consequently activates p53, leading to p21 transcription and the induction of cellular senescence. Treatment with doxorubicin (Dox) or nutlin-3a further enhances p53-mediated transcriptional activation of p21, and their combination with LTβR depletion exerts an additive effect in promoting cellular senescence.
    DOI:  https://doi.org/10.1038/s41420-025-02708-1
  5. J Med Chem. 2025 Sep 04.
      The blocking interaction between p53 and its negative regulator MDM2 is an engaging therapeutic strategy for antitumor drug development, and there are several drug candidates of p53-MDM2 inhibitors in clinical trials. In the present study, novel drug conjugates of p53-MDM2 inhibitors and topoisomerase I (TOP1) inhibitors have been designed based on bioinformatics analysis results of ten tumor tissues. Among them, ZM484 showed potent antiproliferative activity against three cell lines HCT116, SJSA-1, and A549, with the strongest p53-MDM2 and TOP1 inhibitory activity. Additionally, the treatment of compound ZM484 significantly reduced the tumor growth of HCT116 in BALB/c nude mice mode. Furthermore, our data highlighted the superior stability and good pharmacokinetic properties of compound ZM484. Using LC-MS analysis, we identified that compound ZM484 is capable of effectively releasing camptothecin (CPT) and the potent p53-MDM2 inhibitor 8a upon coincubation with DTT. Therefore, compound ZM484 could be a potential drug-conjugate candidate for the treatment of colorectal cancer.
    DOI:  https://doi.org/10.1021/acs.jmedchem.5c01003
  6. bioRxiv. 2025 Aug 31. pii: 2025.08.28.672283. [Epub ahead of print]
      Acute myeloid leukemia (AML) is a heterogeneous disease characterized by a broad spectrum of molecular alterations that influence clinical outcomes. TP53 mutations define one of the most lethal subtypes of acute myeloid leukemia (AML), driving resistance to nearly all available treatment modalities, including venetoclax plus azacitidine (VenAza). Yet, the molecular basis of this resistance, beyond affecting transactivation of BCL-2 family genes, has remained elusive. Here, we demonstrate that VenAza treatment leads to reduced transcriptional upregulation of the p53 signaling pathway in TP53 mutant/deficient AML compared to wild-type AML. Functionally, TP53 mutant/deficient AML exhibits selective failure in apoptosis induction rather than impaired G1 arrest or senescence. Despite inhibition of pro-apoptotic BAX and selective enrichment for MCL-1 in TP53 mutant isogenic AML cells, compensatory upregulation of BIM preserved functional mitochondrial outer membrane permeabilization (MOMP). TP53 mutant primary AML tumors at baseline also had retained capacity for MOMP. Instead, TP53 mutant AML exhibited disruption in caspase-3/7 activation to evade apoptosis after VenAza therapy, decoupling the mitochondrial and executioner phases of apoptosis. Importantly, this (post-MOMP brake) is not a bystander effect but itself a driver of VenAza and chemotherapy resistance in TP53 mutant/deficient AML. This previously unrecognized mechanistic insight shifts the focus from mitochondrial priming to terminal caspase blockade in TP53 mutant AML and opens the door for urgently needed therapeutic strategies that reignite apoptosis at its execution point.
    DOI:  https://doi.org/10.1101/2025.08.28.672283