Liora Wittle

Chem Biomed Imaging. 2025 Dec 29;4(5):912-923. doi: 10.1021/cbmi.5c00207. eCollection 2026 May 25.

ABSTRACT

Strain-promoted azide-alkyne cycloaddition (SPAAC) reactions between azides and strained alkynes are some of the most widely used bioorthogonal reactions for molecular imaging applications, such as in positron emission tomography (PET). Radiolabeled azides and alkynes have been developed for click reactions; however, very few compounds have been studied in the intracellular space, where stability, selectivity, and reactivity may be affected by the surrounding complex intracellular environment. Motivated by the lack of tools to evaluate azide tracer candidates for bioorthogonal click reactions in the intracellular compartment, we designed and synthesized Hoechst-DBCO, a Hoechst 33258 derivative that accumulates in cells. Hoechst 33258 has strong DNA binding properties and is used as a courier to deliver dibenzocyclooctyne (DBCO), a strained alkyne, into the nucleus to track click reactions in living cells. The ultimate aim of this study was to develop an in vitro assay to detect and investigate specific SPAAC bioorthogonal click reactions in living cells and to evaluate permeability, uptake, and reactivity in the intracellular compartment. The Hoechst-DBCO compound we developed can help accelerate the evaluation of candidates for bioorthogonal click reactions and find suitable radiopharmaceuticals for imaging procedures.

PMID:42222556 | PMC:PMC13217358 | DOI:10.1021/cbmi.5c00207

Carbohydr Polym. 2026 Aug 1;385:125392. doi: 10.1016/j.carbpol.2026.125392. Epub 2026 May 2.

ABSTRACT

Hydrogels are attractive scaffolds for regenerative medicine, yet few systems combine robust mechanical performance, antimicrobial functionality, and controlled bioactivity. Here, we engineered chitosan-based hydrogels crosslinked via strain-promoted azide-alkyne cycloaddition (SPAAC) using 4-arm PEG-DBCO and functionalized with NeoNectin, a de novo-designed protein exhibiting subnanomolar affinity and high specificity for integrin α5β1. Rheological analysis confirmed stable hydrogel formation with an elastic modulus of ∼0.1 kPa, within the physiological range of bone marrow and typically associated with maintenance of mesenchymal stem cells (MSCs) in an undifferentiated state, enabling evaluation of integrin-specific biochemical cues in an inhibitory mechanical environment. Antimicrobial assays confirmed intrinsic bactericidal activity against Staphylococcus aureus and Pseudomonas aeruginosa, mitigating infection risks associated with implantation. Encapsulated human MSCs maintained high viability across all groups, validating cytocompatibility of the SPAAC crosslinking. Importantly, only covalently immobilized NeoNectin promoted sustained proliferation, increased expression of osteogenic genes, and significantly enhanced alkaline phosphatase activity, despite the low stiffness of the hydrogel matrix. These findings demonstrate that α5β1-specific signaling can override mechanical cues and drive osteogenic differentiation within ultra-soft environments. Overall, NeoNectin-functionalized SPAAC hydrogels provide a multifunctional platform that integrates antimicrobial properties, mechanical stability, and cell-instructive signaling for bone regeneration and broader tissue engineering applications.

PMID:42173590 | DOI:10.1016/j.carbpol.2026.125392

Int J Mol Sci. 2026 May 16;27(10):4478. doi: 10.3390/ijms27104478.

ABSTRACT

Candida albicans is the causal agent of invasive candidiasis, which might be lethal in immunocompromised patients. Biofilm formation is considered a key virulence factor of C. albicans and is associated with its elevated resistance to antifungals. C. albicans and bacteria like E. coli are frequently found to form mixed biofilms on biotic or abiotic surfaces, rendering them more refractory to existing antifungals. To investigate how E. coli endogenous indole interplaying with exogenous IAA exerts modulatory effects on dual-species biofilm with C. albicans, an E. coli strain deficient in the indole biosynthetic gene tnaA was constructed, and the enzyme TnaA inhibitor was administered to block the indole production in E. coli monoculture and/or E. coli-C. albicans dual culture. Phenotypic assay revealed that indole deficiency attenuated E. coli mono-species biofilm by 12% (tnaA∆ versus WT E. coli), and the lack of indole in the E. coli cell-free culture filtrate abolished the ability to promote C. albicans biofilms, evidenced by the fact that the treatment with WT E. coli culture supernatants exhibited a 1.7-fold promotive effect, while treatment with tnaA∆ displayed no significant difference from the broth control towards C. albicans biofilms. Furthermore, impaired E. coli indole production might disrupt E. coli-C. albicans biofilm, as examined by confocal laser scanning microscopy (CLSM). Moreover, indole-3-acetic acid (IAA) was found to exhibit more potent biofilm-modulatory activity than indole by CLSM imaging with dual biofilms of WT E. coli-C. albicans, in contrast to those of E. coli tnaA∆-C. albicans post-supplemented with exogenous IAA. This study provides evidence for indole as a signaling molecule mediating bacterial-fungal communication during mixed-biofilm formation. Indole and its derivatives, particularly in combination with existing antifungals, have potential in the development of anti-biofilm strategies to eradicate refractory fungal infections.

PMID:42196465 | PMC:PMC13208022 | DOI:10.3390/ijms27104478

Commun Biol. 2026 May 14. doi: 10.1038/s42003-026-10260-6. Online ahead of print.

ABSTRACT

Methicillin-resistant Staphylococcus aureus (MRSA) poses a persistent clinical threat due to limited therapeutic options and the rapid emergence of resistance. Azeliragon, an orally bioavailable Receptor for Advanced Glycation End-products (RAGE) inhibitor previously tested in human trials, was identified as a potential antibacterial agent against MRSA through high-throughput screening. It exhibited potent antibacterial activity against clinical S. aureus isolates (MIC₅₀ = 6.25 μM/3.3 μg/mL) and significantly inhibited biofilm formation. Metabolomics and proteomics suggested perturbation of lipid pathways and potential interaction with MurA. Target validation using Drug Affinity Responsive Target Stability (DARTS), Determination of biomolecular affinity by bio-layer interferometry (BLI), Limited proteolysisemass spectrometry (LiP-MS), and site-directed mutagenesis provided biochemical evidence supporting MurA as an intracellular target. Whole Genome Sequencing of resistant derivatives revealed Single Nucleotide Polymorphisms (SNPs) in cell-wall and fatty-acid efflux regulators including yycH, farE/farR, consistent with membrane and cell-wall perturbation. In a murine wound model Azeliragon reduced local bacterial burden and accelerated healing to levels comparable with vancomycin. Azeliragon is a repurposable antibacterial agent that perturbs membrane phospholipid homeostasis and engages MurA-dependent peptidoglycan synthesis. These findings support further preclinical development of Azeliragon or optimized derivatives as potential therapeutics against MRSA and other gram-positive pathogens.

PMID:42135462 | DOI:10.1038/s42003-026-10260-6

medRxiv [Preprint]. 2026 May 6:2026.05.05.26352475. doi: 10.64898/2026.05.05.26352475.

ABSTRACT

Lyme disease is a growing and prominent human health problem caused by a group of spirochaetal bacteria that belong to the Borrelia genus. Persistent Lyme disease infection produces a multi-system disorder that may result in severe arthritis, carditis, neurological problems, and even death. Preventing severe disease requires immediate treatment, but current approaches to diagnose Lyme disease are indirect, serology-based assays that may fail early in infection. All Lyme disease-causing Borrelia species shed distinct and unique fragments of their peptidoglycan cell wall during growth. We exploited this fundamental biological process to develop an acute, urine-based diagnostic test. Using a cocktail of unique and highly specific monoclonal antibodies, our ELISA-mediated approach accurately reports on the status of an active, acute infection, in a laboratory animal model of Lyme disease, as well as humans. This rapid, simple, and innovative approach detects an active infection in as few as 3 days of transmission and in 88% of human patients yet to seroconvert-more than ∼2 weeks before serology would be positive.

PMID:42145611 | PMC:PMC13174708 | DOI:10.64898/2026.05.05.26352475

Microb Genom. 2026 May;12(5):001723. doi: 10.1099/mgen.0.001723.

ABSTRACT

Tuberculosis (TB), caused by Mycobacterium tuberculosis, is one of the world's deadliest diseases, currently responsible for ~1.5 million deaths per year and rising. Recently, rifampicin-resistant M. tuberculosis was designated as a critical priority pathogen status by the World Health Organization. However, few controlled laboratory studies are available that systematically assess the molecular drivers of antibiotic resistance development in TB. In this study, we paired laboratory-directed evolution and population-level deep-sequencing approaches to map the evolutionary pathways taken by M. tuberculosis to develop resistance to first- and last-line therapies (rifampicin and linezolid) and then characterized de novo resistance mutation occurrence over time. We demonstrated that the majority of M. tuberculosis populations readily acquire mutations in genes commonly found in rifampicin- and linezolid-resistant clinical isolates (rpoB and rplC). However, we also identified mutations in six genes, mostly present in subpopulations (17-41%) and not previously linked to rifampicin or linezolid resistance, including four associated with rifampicin resistance (Rv0052, ppsD, ppsE and mptC) and two associated with linezolid resistance (glpK and echA12). The ppsD, glpK and mptC mutations were also identified in published individual sequencing reads of antibiotic-resistant clinical isolates. Further investigation of the identified resistance determinants ppsD/E established that mutations in these genes appear to mediate resistance across multiple species, with an Escherichia coli mutant of the ortholog (fabF), representing a shared domain featured in PpsD and PpsE, phenotypically displaying increased antibiotic tolerance to low-level rifampicin. This study highlights the power of using controlled laboratory studies to uncover minority variants in populations of M. tuberculosis. These outcomes will lead to improved diagnosis of antibiotic resistance emergence in TB, to optimize management and treatment of TB infections, and ultimately to minimize patient deaths.

PMID:42154617 | PMC:PMC13186403 | DOI:10.1099/mgen.0.001723

Proc Natl Acad Sci U S A. 2026 May 26;123(21):e2531588123. doi: 10.1073/pnas.2531588123. Epub 2026 May 19.

ABSTRACT

Resistance to immune checkpoint blockade (ICB) often arises from immunologically cold tumors enriched in suppressive myeloid cells. Previous studies have implicated NOD2 signaling in antitumor immunity and in modulation of ICB responses, but approaches to engage this pathway effectively and durably within tumors remain limited. Here, single-cell transcriptomic analysis of colorectal cancer identified a NOD2^high tumor-associated macrophage (TAM) subset enriched for inflammatory and immune-activating programs. To therapeutically harness this state, we engineered an injectable manganese-containing alginate hydrogel encapsulating polyarginine-functionalized Bacillus Calmette-Guérin (MHY@PBCG) for sustained intratumoral delivery and localized coactivation of NOD2 and STING signaling in TAMs. Polyarginine enhanced BCG uptake by macrophages, whereas Mn²⁺ stabilized the hydrogel and amplified STING activation. Local administration of MHY@PBCG reprogrammed TAMs toward an M1-like phenotype, increased inflammatory cytokine and interferon programs, converted cold tumors into immune-inflamed lesions, and restored responsiveness to anti-PD1 therapy in multiple models. Mechanistically, coordinated NOD2/STING activation established a self-reinforcing inflammatory circuit linking macrophage reprogramming to downstream T cell-mediated antitumor immunity. These findings establish a localized biomaterial strategy for overcoming checkpoint resistance through macrophage-centered remodeling of the tumor microenvironment.

PMID:42154546 | PMC:PMC13213998 | DOI:10.1073/pnas.2531588123

Ann Biomed Eng. 2026 May 12. doi: 10.1007/s10439-026-04152-3. Online ahead of print.

ABSTRACT

PURPOSE: To develop and validate a bioorthogonal labeling approach for quantifying ECM remodeling in living cell and tissue culture systems.

METHODS: Strain-promoted azide-alkyne (SPAAC) reactions, or copper-free click chemistry, were used to fluorescently label newly synthesized glycan and protein matrix components. ECM synthesis and degradation was quantified in cartilage explants, human mesenchymal stem cells, and SKBR3 breast cancer cells under various external stimuli, including inflammation, mechanical stimulus, and drug treatment.

RESULTS: The click chemistry method reliable quantified ECM turnover across platforms. It detected reduced glycan and protein synthesis after 24-hour inflammatory challenge and enabled longitudinal tracking of ECM degradation in cartilage explants. The technique demonstrated high sensitivity, measuring increased ECM deposition by ~ 10,000 human mesenchymal stem cells in 12-hour intervals and substrate stiffness-dependent synthesis by SKBR3 cells. Additionally, the approach supported osteoarthritis drug screening by identifying compounds that mitigated inflammation-induced ECM degradation.

CONCLUSION: Compared to traditional biochemical or histological assays, the click chemistry-based technique provides higher sensitivity, reduced sample requirements, and improved temporal resolution for quantifying ECM turnover. Its versatility enables broad application in tissue engineering, regenerative medicine, disease modeling, and high-throughput drug evaluation.

PMID:42120803 | DOI:10.1007/s10439-026-04152-3

Sci Adv. 2026 May 8;12(19):eaeb6691. doi: 10.1126/sciadv.aeb6691. Epub 2026 May 8.

ABSTRACT

Nascent adhesions are early integrin-based assemblies that couple the extracellular matrix to the actin cytoskeleton and mature into focal adhesions. Many nascent-adhesion proteins interact through weak, multivalent contacts, suggesting that liquid-like organization may contribute to adhesion assembly. However, how phase separation shapes actin polymerization and organization remains unclear. Here, we compare two vasodilator-stimulated phosphoprotein (VASP)-recruiting adaptor proteins, zyxin and vinculin, to determine how adaptor identity tunes condensate properties and actin coupling. Both zyxin-VASP and vinculin-VASP assemblies drive integrin clustering and support actin filament growth. Notably, zyxin-VASP condensates remain fluid and redistribute along newly formed actin bundles, whereas vinculin-VASP condensates are more rigid and fail to spread along actin despite sustaining polymerization. These results suggest that differential VASP recruitment can modulate condensate properties and actin architecture, providing a potential mechanism for the maturation of nascent adhesions into focal adhesions.

PMID:42102206 | PMC:PMC13155341 | DOI:10.1126/sciadv.aeb6691

J Am Chem Soc. 2026 May 12. doi: 10.1021/jacs.6c04860. Online ahead of print.

ABSTRACT

Lipid asymmetry was probed in supported lipid bilayers (SLBs) formed by vesicle fusion on planar glass substrates and protein-coated substrates. Leaflet distribution was determined via fluorescence microscopy following bilayer unzipping. Each SLB was primarily composed of phosphatidylcholine (PC) with 0.5 mol % of a test lipid containing a tail-labeled probe. At equilibrium, the results revealed that 75% of labeled phosphatidylserine (PS) and phosphatidylethanolamine (PE) lipids partitioned into the lower leaflet adjacent to the glass surface. This preferential partitioning further increased when experiments were conducted in D₂O rather than an H₂O buffer, a finding consistent with favorable hydrogen bond (H-bond) formation between surface silanols on the glass support and the headgroups of PS and PE lipids. In fact, H-bonding was the dominant factor in determining the interleaflet distribution. Varying the salt concentration could modulate the PS fraction in only the lower leaflet by a small amount, ±3%. A tail-labeled PC probe, which was unable to donate an H-bond to the surface, showed no preference for the lower leaflet once its equilibrium distribution was achieved. Finally, the 2D diffusion of the PS and PE probes, but not PC, was strongly dependent on the number of available H-bonding sites on the substrate surface. These results are reminiscent of the lipid asymmetry observed in the plasma membranes of living cells, where PS and PE are similarly partitioned into the inner leaflet, suggesting that the H-bonding environment in the cytoplasmic versus extracellular region may play a significant role in governing lipid asymmetry in vivo.

PMID:42118149 | DOI:10.1021/jacs.6c04860

Brain Behav Immun. 2026 May 11:106803. doi: 10.1016/j.bbi.2026.106803. Online ahead of print.

ABSTRACT

This narrative review discusses mechanisms underlying bidirectional communication between sleep and the immune system with a focus on innate immune signaling and neuroinflammatory processes. Decades of mechanistic research demonstrate that sleep and immune function are tightly integrated across molecular, cellular, and systems levels. Seminal experiments from the late 1960 s through the early 1980 s established that microbial products, such as muramyl peptides and lipopolysaccharide, along with cytokines including IL-1 and TNF, alter sleep and participate in its physiological regulation. These findings launched contemporary investigations into how innate immune receptors, PAMP recognition, and downstream inflammatory signaling shape sleep-wake architecture. More recent work demonstrates that acute or chronic sleep disruption-including deprivation, restriction, and fragmentation-activates inflammatory signaling pathways, alters cytokine expression, and induces neuroinflammatory responses within the brain. At the cellular level, glial cells play central roles in mediating these effects and linking immune activation to neuronal circuits regulating sleep-wake behavior. Together, these advances reveal that sleep-immune interactions are deeply integrated and critical for maintaining health.

PMID:42119911 | DOI:10.1016/j.bbi.2026.106803

Proc Natl Acad Sci U S A. 2026 May 5;123(18):e2519981123. doi: 10.1073/pnas.2519981123. Epub 2026 Apr 29.

ABSTRACT

Inflammatory injury to the intestine triggers a reprogramming of the intestinal epithelium to a fetal-like state that drives rapid restoration of the epithelial barrier. Although the intestinal microbiota is a key modulator of inflammation, its role in influencing epithelial fetal-like stem cell reprogramming and consequent restitution remains unclear. Using irradiation (IR) injury as a model for small intestinal epithelium injury and repair, we found that the intestinal microbiota accelerated epithelial restitution by amplifying a repair-associated inflammatory response that promoted the emergence of fetal-like intestinal epithelial cells (IECs), marked by Ly6a and Clu. NOD2, the strongest genetic link to the development of Crohn's disease, was found to be expressed in fetal-like IECs following injury. Employing an ileal organoid model, we demonstrated that NOD2 activation by its peptidoglycan ligand potentiated an inflammatory gene signature characterized by interferon signaling, concurrent with enterocyte recovery. NOD2 deficiency exacerbated epithelial apoptosis following IR injury, whereas epithelial-specific NOD2 signaling promoted fetal-like IEC emergence and increased epithelial proliferation. Collectively, these findings reveal a pivotal role for the microbiota and NOD2-mediated microbial sensing in regulating fetal-like IEC fate after injury, thus contributing to the protective function of this microbial sensor during intestinal inflammation.

PMID:42054366 | PMC:PMC13143025 | DOI:10.1073/pnas.2519981123

Biointerphases. 2026 Mar 1;21(2):020801. doi: 10.1116/6.0005379.

ABSTRACT

The Langmuir monolayer technique has proven to be an effective method for constructing lipid-based models of cell membranes. Compared to other artificial membrane systems, such as liposomes or supported lipid bilayers, it offers a relatively simple and versatile approach to reconstructing lipid components of biological membranes and systematically modifying their composition. The technique allows precise control over experimental parameters such as surface pressure and temperature, which influence the physical state and organization of lipid monolayers. Lipid monolayer models are widely used to investigate molecular interactions at membrane interfaces, including the effects of biomolecules or xenobiotics on membrane properties, identification of potential molecular targets of drugs, and evaluation of mechanisms underlying their pharmacological activity or toxicity. While the successful application of the monolayer technique in lipid membrane modeling has been extensively reported in the literature, comprehensive discussions of lipid compositions for modeling various membrane types-such as eukaryotic, prokaryotic, viral, and pathological membranes-remain limited. In particular, systematic descriptions of lipid mixtures used to model membranes characteristic of eukaryotic cells, prokaryotes, viruses, or pathological states are limited. The aim of this review is to address this gap by summarizing lipid compositions used in Langmuir monolayer models designed to mimic different biological membrane types.

PMID:42030177 | DOI:10.1116/6.0005379

Bio Protoc. 2026 Apr 20;16(8):e5656. doi: 10.21769/BioProtoc.5656. eCollection 2026 Apr 20.

ABSTRACT

The spatiotemporal dynamics and density of actin networks are key determinants of actin cytoskeleton-mediated cellular functions. In vitro reconstitution systems have been widely used to study actin cytoskeletal dynamics; however, many existing approaches offer limited flexibility in controlling the geometry, thickness, and density of the assembled actin networks. Here, we present an in vitro optogenetic protocol that enables precise control of actin network assembly on supported lipid bilayers using an improved light-induced dimer (iLID)-SspB-based light-inducible dimerization system. In this system, His-mEGFP-iLID is anchored to a Ni-NTA-containing lipid bilayer, while SspB-mScarlet-I-VCA, a nucleation-promoting factor fused with SspB, together with other actin cytoskeletal proteins, is supplied in bulk solution. Upon blue light illumination, SspB-mScarlet-I-VCA is recruited to the membrane in a spatially and temporally defined manner, inducing localized actin polymerization. By tuning illumination patterns and duration, actin networks with defined density, thickness, and geometry can be generated, and polymerization can be rapidly halted by stopping illumination. This protocol provides a versatile platform for reconstructing actin networks with controlled spatial organization and density, enabling quantitative analysis of density-dependent interactions between actin networks and actin-binding proteins. Key features • Actin networks with varying densities and arbitrary shapes can be formed on the same supported lipid bilayer by controlling blue light illumination through the objective lens. • Actin polymerization can be stopped simply by turning off blue light illumination, enabling the formation of actin networks with defined thicknesses. • This protocol requires purified actin and actin-binding proteins.

PMID:42037760 | PMC:PMC13103897 | DOI:10.21769/BioProtoc.5656

Proc Natl Acad Sci U S A. 2026 May 12;123(19):e2528400123. doi: 10.1073/pnas.2528400123. Epub 2026 May 5.

ABSTRACT

Biomembranes are complex two-dimensional liquids composed of hundreds of lipid species that interact in a myriad of ways. One such interaction, that between sphingomyelin (SM) and cholesterol in plasma membranes of animal cells, provides many functional benefits, including protection from microbial infection, prevention of unrestrained cell growth, and proper maintenance of cellular lipid composition. Owing to the liquid nature of membranes, the structure of the SM/cholesterol interaction, or any other functionally critical lipid-lipid interaction, has remained elusive. Here, we overcome this challenge using a fungal toxin called Ostreolysin A (OlyA), that has been shown to specifically bind to SM/cholesterol complexes in membranes. We used OlyA to stabilize the SM/cholesterol interaction much in the same way as antibodies are used to stabilize preexisting protein complexes. Cryoelectron microscopy analysis of OlyA bound to SM/cholesterol membranes reveals the details of the tight interaction between these two lipids-the steroid nucleus of cholesterol packs against the acyl chains of SM, and a hydrogen bond forms between the nitrogen on SM's ceramide base and the oxygen on cholesterol's hydroxyl group, thus sequestering this key functional group of cholesterol. The importance of hydrogen bonding in stabilizing the SM/cholesterol interaction is supported by structural analysis of a mutant form of OlyA that binds free SM in a cholesterol-independent manner. These results provide structural insights into the organization of cholesterol in membranes.

PMID:42085157 | PMC:PMC13167793 | DOI:10.1073/pnas.2528400123

ACS Omega. 2026 Apr 10;11(15):22766-22786. doi: 10.1021/acsomega.5c11987. eCollection 2026 Apr 21.

ABSTRACT

Autoantibodies (AABs) are valuable biomarkers for diagnosing and monitoring autoimmune diseases and cancer. Conventional AAB profiling methods, such as enzyme-linked immunosorbent assay and immunoblot, are time-consuming, labor-intensive, and limited in multiplexing capacity. Luminex xMAP technology overcomes these limitations by enabling high-throughput, multiplexed AAB detection via bead-based immunoassays. However, the random immobilization of antigens on Luminex beads can lead to suboptimal epitope exposure, reduced binding sensitivity, and inconsistent assay performance. This study examines whether oriented antigen immobilization via genetic code expansion and click chemistry enhances binding sensitivity on the Luminex platform compared to random immobilization via conventional amine coupling. We selected three human antigenic proteins, HDAC3, RPS17, and RPS4Y1, and incorporated the noncanonical amino acid (ncAA) N ^ε-((2-azidoethoxy)-carbonyl)-l-lysine (AzK) at a genetically defined position using the stop codon suppression method. This enabled site-specific conjugation of the antigens to dibenzocyclooctyne (DBCO)-functionalized beads via strain-promoted azide-alkyne cycloaddition (SPAAC). Binding sensitivity was assessed using serum samples from 88 individuals (22 healthy and 66 lung carcinoma patients). Oriented immobilization of RPS4Y1 AzK on DBCO-beads resulted in a 2.5-fold increase in binding sensitivity compared to random immobilization on COOH-beads, demonstrating that controlled antigen orientation improves epitope accessibility and enhances AAB detection sensitivity. These findings establish site-specific antigen immobilization via genetic code expansion and click chemistry as a superior alternative to conventional amine coupling. This immobilization approach significantly improves AAB detection and holds broad potential for applications such as antibody profiling, diagnostics, and drug screening on the Luminex and other biosensing and diagnostics platforms, where high sensitivity and accuracy are essential.

PMID:42040488 | PMC:PMC13103837 | DOI:10.1021/acsomega.5c11987