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Dal Molin, M.

Publications and source records attributed to Dal Molin, M..

3 recordsLinked to original sources

Spatial Regulation of CAR Signaling Enables Logic-Gated Activity

Chimeric antigen receptors (CARs) can induce T cells to kill cancer cells but also to kill normal cells that express the same antigens1. Designing CARs to recognize combinations of antigens, via Boolean logic, can simultaneously expand the scope of targetable antigens and make CAR T cells more specific to cancer2. For example, one antigen may be expressed on cancer cells and normal bone marrow cells, while a second antigen may be present on the same cancer cells but only in normal lungs. If recognition of both antigens is required for T cell activation, only the cancer cells will be killed. Creating such AND-gated CAR T cells has been challenging given the need to engineer non-natural signaling mechanisms that integrate two ligand binding events into a single T cell activation stimulus3-6. Here, we design a fundamentally new AND-gated receptor called Multi-ANtigen Triggered Immune Synapse (MANTIS), which leverages differences in extracellular receptor dimensions to regulate CAR signaling. MANTIS initially prevents CAR activity by steric blocking with a bulky extracellular domain. Upon engagement of the first antigen, MANTIS sheds this blocking domain, releasing a free CAR that can bind a second antigen and activate the T cell in an AND-gated manner. This work demonstrates how differences in extracellular receptor size can be leveraged to spatially regulate intracellular signaling pathways in response to antigen patterns, paving the way for new applications in synthetic biology and cell engineering. One sentence summaryDifferences in extracellular size can be leveraged to regulate CAR T cell activity for precise recognition of antigen patterns.

synthetic biology↗

Enabling antibiotic research: towards selective peptide deformylase inhibitors

Peptide deformylase plays a crucial role in prokaryotic translation and constitutes an antibiotic target previously addressed in clinical trials. In eukaryotes, mitochondrial translation also relies on peptide deformylase, necessitating antibiotic development to aim for selective inhibition of the bacterial enzymes. In the present study, we investigated two compound series: derivatives of actinonin and compounds containing a 5-bromoindole scaffold. Antibacterial activity was evaluated by microdilution-based minimal inhibitory concentration assay and selectivity investigated using human peripheral blood mononuclear cells. In vitro peptide deformylase inhibition was compared for the Escherichia coli and human enzyme. To validate peptide deformylase inhibition in vivo, a mass spectrometric analysis directly coupled to the minimal inhibitory concentration assay was developed for the model organism Bacillus subtilis. Two compounds originating from this work (ZHO-119, ZHO-197) showed antibacterial activity comparable to actinonin, and for the comparator compound BB-3497 superior anti-gram-negative and anti-tubercular activity was confirmed. The three compounds displayed no cytotoxicity and were equally selective in vitro for the bacterial enzyme. The mass spectrometry-based analysis indicates that in addition to peptide deformylase, ZHO-197 very effectively inhibits bacterial methionine aminopeptidase, the metallo-enzyme that removes the deformylated N-terminal methionine.

microbiology↗

ME3BP-7 is a targeted cytotoxic agent that rapidly kills pancreatic cancer cells expressing high levels of monocarboxylate transporter MCT1

Nearly 30% of Pancreatic ductal adenocarcinoma (PDAC)s exhibit a marked overexpression of Monocarboxylate Transporter 1 (MCT1) offering a unique opportunity for therapy. However, biochemical inhibitors of MCT1 have proven unsuccessful in clinical trials. In this study we present an alternative approach using 3-Bromopyruvate (3BP) to target MCT1 overexpressing PDACs. 3BP is a cytotoxic agent that is known to be transported into cells via MCT1, but its clinical usefulness has been hampered by difficulties in delivering the drug systemically. We describe here a novel microencapsulated formulation of 3BP (ME3BP-7), that is effective against a variety of PDAC cells in vitro and remains stable in serum. Furthermore, systemically administered ME3BP-7 significantly reduces pancreatic cancer growth and metastatic spread in multiple orthotopic models of pancreatic cancer with manageable toxicity. ME3BP-7 is, therefore, a prototype of a promising new drug, in which the targeting moiety and the cytotoxic moiety are both contained within the same single small molecule. One Sentence SummaryME3BP-7 is a novel formulation of 3BP that resists serum degradation and rapidly kills pancreatic cancer cells expressing high levels of MCT1 with tolerable toxicity in mice.

cancer biology↗