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Here, we present remarkable epoxyketone-based proteasome inhibitors with low nanomolar in vitro potency for blood-stage Plasmodium falciparum and low cytotoxicity for human cells. Our best compound has more than 2,000-fold greater selectivity for erythrocytic-stage P. falciparum over HepG2 and H460 cells, which is largely driven by the accommodation of the parasite proteasome for a D-amino acid in the P3 position and the preference for a difluorobenzyl group in the P1 position. We isolated the proteasome from P. falciparum cell extracts and determined that the best compound is 171-fold more potent at inhibiting the β5 subunit of P. falciparum proteasome when compared to the same subunit of the human constitutive proteasome. These compounds also significantly reduce parasitemia in a P. berghei mouse infection model and prolong survival of animals by an average of 6 days. The current epoxyketone inhibitors are ideal starting compounds for orally bioavailable anti-malarial drugs.
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http://dx.doi.org/10.1002/chem.202203958 | DOI Listing |
J Biomed Sci
September 2025
Department of Biochemistry, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo, Japan.
Background: PPM1D (protein phosphatase Mg⁺/Mn⁺ dependent 1D) is a Ser/Thr phosphatase that negatively regulates p53 and functions as an oncogenic driver. Its gene amplification and overexpression are frequently observed in various malignancies and disruption of PPM1D degradation has also been reported as a cause of cancer progression. However, the precise mechanisms regulating PPM1D stability remain to be elucidated.
View Article and Find Full Text PDFElife
September 2025
Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, India.
The UFD-1 (ubiquitin fusion degradation 1)-NPL-4 (nuclear protein localization homolog 4) heterodimer is involved in extracting ubiquitinated proteins from several plasma membrane locations, including the endoplasmic reticulum. This heterodimer complex helps in the degradation of ubiquitinated proteins via the proteasome with the help of the AAA+ATPase CDC-48. While the ubiquitin-proteasome system is known to have important roles in maintaining innate immune responses, the role of the UFD-1-NPL-4 complex in regulating immunity remains elusive.
View Article and Find Full Text PDFJ Med Chem
September 2025
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, California 92093, United States.
Proteasome inhibitors are effective in treating hematologic cancers but have limited utility in brain tumors due to poor blood-brain barrier (BBB) penetration and metabolic instability. In this study, we developed novel macrocyclic peptide epoxyketone inhibitors with improved drug-like properties. Compounds were screened for cytotoxicity against brain cancer cell lines, permeability (PAMPA-BBB and Caco-2), and metabolic stability.
View Article and Find Full Text PDFEur J Pharmacol
September 2025
Departamento de Química and Institute for Advanced Research in Chemical Science (IAdChem), Facultad de Ciencias, Módulo 13, Universidad Autónoma de Madrid, 28049, Madrid, Spain.
The Skp2-Cks1 protein-protein interaction (PPI) within the SCF ubiquitin ligase acts as a co-receptor for phosphorylated CDK inhibitors-most prominently p27-relieving CDK inhibition and advancing the cell cycle, a dependency accentuated in RB-pathway-defective cancers. Crystallographic and cryo-EM analyses delineate a composite pocket formed by the Skp2 leucine-rich-repeat groove and the phosphate-recognition site of Cks1; Cks1-centered open-closed motions further influence druggability. Using HTRF/TR-FRET and AlphaScreen biochemistry, alongside cell-based target-engagement readouts in some studies, three small-molecule classes have emerged that disrupt this PPI: 1,3-diphenyl-pyrazines and triazolo[1,5-a]pyrimidines (lead E35) with low-micromolar potency, and "Skp2E3LI" compounds with micromolar cellular activity.
View Article and Find Full Text PDFArch Pharm Res
September 2025
College of Pharmacy, Hanyang University, Ansan, 15588, Republic of Korea.
c-Jun N-terminal kinases (JNKs), a subfamily of mitogen-activated protein kinases (MAPKs), are key mediators of cellular responses to environmental stress, inflammation, and apoptotic signals. The three isoforms-JNK1, JNK2, and JNK3 exhibit both overlapping and isoform-specific functions. While JNK1 and JNK2 are broadly expressed across tissues and regulate immune signaling, cell proliferation, and apoptosis, JNK3 expression is largely restricted to the brain, heart, and testis, where it plays a crucial role in neuronal function and survival.
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