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Nambiar, D.

Publications and source records attributed to Nambiar, D..

3 recordsLinked to original sources

3D Spatial Interactomics Maps the Dynamics of NF-κB Multiprotein Signalosomes in Single Cells

NF{kappa}B signaling drives inflammatory responses by rapidly assembling membrane-proximal multiprotein supercomplexes, yet how these assemblies are organized in space and time within the 3D interior of a single cell has remained uncharacterized. We addressed this by profiling endogenous NF{kappa}B protein-protein interactions with an intelligent sequential proximity ligation assay (iseqPLA), read out by spinning disk confocal microscopy and 3D reconstruction. Each detected protein-protein proximity event is represented by a rolling-circle amplification product, and we treat clusters of co-localized puncta as a measure of supercomplex spatial organization. Across NIH-3T3 mouse fibroblasts, cystic fibrosis (CF) patient-derived macrophage co-cultures with IMR-90 human fibroblasts, and an independent set of healthy- and CF-donor monocyte-fibroblast co-cultures profiled by 3D iseqPLA, we tracked supercomplex dissociation, p65 nuclear translocation, and negative-feedback engagement across cytokine time courses. Three findings emerge: 3D volumetric quantification reduces the variance in nuclear-to-cytoplasmic ratio measurements relative to 2D projections, the choice of extracellular matrix coating shapes the fraction of NF{kappa}B-responsive cells, and CF airway-conditioned macrophages amplify paracrine NF{kappa}B signaling in neighboring fibroblasts in a CF model. A single-cell Generative Pretrained Transformer (scGPT) foundation model, fine-tuned on curated transcriptomic datasets, further places our NF{kappa}B gene panel within an inflammation-relevant feature space. Together, these results establish a 3D spatial interactomics workflow for dissecting supercomplex dynamics in health and disease.

bioengineering↗

Biodistribution-Driven Discovery Identifies a Glycosidase-Cleavable Linker to Reprogram Radiotheranostics

While radiopharmaceutical therapy (RPT) has become part of the standard-of-care for patients with advanced prostate cancers and neuroendocrine tumors (NETs), cures are elusive and normal tissue toxicity remain a challenge. Chemical groups susceptible to cleavage by enzymes present in tumors, tumor microenvironment or in normal tissues, have the potential to improve the therapeutic index for RPT. Using DOTA-TATE as an example and drawing from strategies used to develop antibody-drug conjugates, we designed, and synthesized, a chemically diverse series of linkers between the chelator (DOTA) and the targeting vector (TATE). Of the 10 agents we tested, two with cleavable linker domains reduced kidney retention compared to DOTA-TATE: the previously reported DOTA-MVK({varepsilon})-TATE, and a novel agent bearing cleavable beta-galactose ({beta}-Gal) unit, DOTA-{beta}-Gal-TATE. In murine models of NETs, positron emission tomography (PET) was used to image yttrium-86 (86Y)-labeled variants and show that, while the 86Y-DOTA-MVK({varepsilon})-TATE exhibits similar tumor uptake to the parent non-cleavable 86Y-DOTA-TATE, 86Y-DOTA-{beta}-Gal-TATE shows enhanced tumor uptake, resulting in up to 10-fold improvement in the tumor-to-kidney ratios compared to 86Y-DOTA-TATE. In vitro and in vivo studies confirm high efficiency, enzyme-specific cleavage of 86Y-DOTA-MVK({varepsilon})-TATE and 86Y-DOTA-{beta}-Gal-TATE, supporting a key role for cleavable linker chemistry in the observed outcomes. RPT studies using actinium-225 (225Ac)-labeled variants confirm that all agents are therapeutically effective and well tolerated. While both cleavable variants exhibit superior local control, overall survival, and more favorable toxicity profile when compared with 225Ac-DOTA-TATE, 225Ac-DOTA-{beta}-Gal-TATE demonstrated lower nephrotoxicity. Our findings suggest a potentially generalizable strategy for improving the pharmacokinetics of radiopharmaceutical therapy agents. One Sentence SummaryA {beta}-galactose-cleavable linker reduces kidney toxicity, enhances tumor targeting and therapeutic efficacy in radiopharmaceutical therapy.

cancer biology↗

Alterations to the broad-spectrum formin inhibitor SMIFH2 improve potency

SMIFH2 is a small molecule inhibitor of the formin family of cytoskeletal regulators that was originally identified in a screen for suppression of actin polymerization induced by the mouse formin Diaphanous 1 (mDia1). Despite widespread use of this compound, it is unknown whether SMIFH2 inhibits all human formins. Additionally, the nature of protein/inhibitor interactions remains elusive. We assayed SMIFH2 against human formins representing six of the seven mammalian classes and found inhibitory activity against all formins tested. We synthesized a panel of SMIFH2 derivatives and found that, while many alterations disrupt SMIFH2 activity, substitution of an electron-donating methoxy group in place of the bromine along with halogenation of the furan ring increases potency by approximately five-fold. Similar to SMIFH2, the active derivatives are also pan-inhibitors for the formins tested. This result suggests that while potency can be improved, the goal of distinguishing between highly conserved FH2 domains may not be achievable using the SMIFH2 scaffold.

biochemistry↗