https://dspace.iiti.ac.in:8080/jspui/handle/123456789/3638 2026-06-24T02:16:54Z 2026-06-24T02:16:54Z Gupta, Sharad Chandra, Sourav https://dspace.iiti.ac.in:8080/jspui/handle/123456789/18391 2026-05-18T09:56:11Z 2026-01-01T00:00:00Z

Title: Lightweight Multimodal CNN for Real-Time Bacterial Classification from Raman Spectroscopy Authors: Gupta, Sharad; Chandra, Sourav Abstract: Delayed pathogen identification is a major driver of inappropriate empirical broad-spectrum antibiotic use and, consequently, antimicrobial resistance (AMR). Conventional culturebased workflows require 24-72 hours, creating a mismatch between diagnostic turnaround and the clinical need for timely, targeted therapy. This paper presents a lightweight multimodal convolutional neural network (CNN) that classifies bacterial species directly from Raman spectra in real time. Unlike existing single-modality approaches, the proposed architecture is the first to jointly process raw one-dimensional spectra and their twodimensional continuous wavelet representations through parallel compact branches, followed by simple feature concatenation. On a three-class bacterial Raman dataset, the network attains 99.13 % test accuracy with only 199 k parameters (0.78 MB) and an average inference time of 1. 5 2 ~ m s per sample, yielding a 164 × speedup over a support vector machine (SVM) baseline while maintaining comparable accuracy. The exceptionally small memory footprint and sub- 2 ms latency make this the first truly deployable model suitable for portable, resource-constrained point-of-care devices, offering a practical route toward rapid, culture-free bacterial diagnostics to support antibiotic stewardship. © 2026 IEEE.

2026-01-01T00:00:00Z Solanki, Kundan Raja, Sk Rameej Samanta, Sunanda Roy, Anjali Kar, Parimal Baig, Mirza Saqib https://dspace.iiti.ac.in:8080/jspui/handle/123456789/18403 2026-05-18T09:56:11Z 2026-01-01T00:00:00Z

Title: Modulating IL-1β-induced pro-atherogenic endothelial responses through drug repurposing Authors: Solanki, Kundan; Raja, Sk Rameej; Samanta, Sunanda; Roy, Anjali; Kar, Parimal; Baig, Mirza Saqib Abstract: Background: Interleukin-1β (IL-1β) plays a central role in driving vascular inflammation and endothelial dysfunction, key processes in the development of atherosclerosis. While biologic therapies targeting IL-1β have shown clinical benefit, their high cost, injectable nature, and potential side effects limit their broader use. Therefore, there is a need to explore more accessible alternatives. In this study, we aimed to identify repurposed small-molecule inhibitors that can effectively modulate IL-1β signaling and protect endothelial function. Methods: We used an integrated strategy combining computational and experimental approaches. Virtual screening, molecular docking, molecular dynamics simulations, and MM-PBSA analyses were performed to identify potential inhibitors targeting IL-1R1. The most promising candidates were then evaluated in vitro using endothelial cell models (HUVEC and EA.hy.926). Their effects were assessed through functional assays, including transendothelial electrical resistance (TEER), VE-cadherin immunofluorescence, and cell viability measurements. Results: Two FDA-approved drugs, radotinib and lomitapide, emerged as strong candidates with high binding affinity and stability toward IL-1R1, outperforming the reference inhibitor anakinra in computational analyses. Experimental validation showed that both compounds effectively reduced IL-1β-induced endothelial dysfunction. They restored barrier integrity, improved TEER values, and maintained VE-cadherin expression and localization. Importantly, both compounds exhibited low cytotoxicity and mitigated IL-1β-driven increases in endothelial permeability. Conclusion: Our findings highlight radotinib and lomitapide as promising repurposed small-molecule inhibitors of IL-1β signaling. By preserving endothelial integrity and dampening inflammatory responses, these compounds may serve as cost-effective and orally available alternatives to current biologic therapies. Further in vivo and mechanistic studies are needed to advance their potential clinical application. © The Author(s), under exclusive licence to Springer Nature Switzerland AG 2026.

2026-01-01T00:00:00Z Chaudhari, Rahul Nigam, Deveish Dasgupta, Mallar Chandravanshi, Khileshwari Malik, Kritika Kodgire, Prashant https://dspace.iiti.ac.in:8080/jspui/handle/123456789/18355 2026-05-14T12:28:26Z 2026-01-01T00:00:00Z

Title: Unraveling the refolding dynamics, TLR2 interaction, and immunomodulatory insights of OmpA from Salmonella Typhimurium Authors: Chaudhari, Rahul; Nigam, Deveish; Dasgupta, Mallar; Chandravanshi, Khileshwari; Malik, Kritika; Kodgire, Prashant Abstract: Salmonella enterica serovar Typhimurium is a Gram-negative bacterium that causes gastrointestinal infection and rising antibiotic resistance worldwide. This study examines the structural-functional relationship of OmpA, a major outer membrane protein (OMP) implicated in Salmonella pathogenesis. Computational analysis revealed a high conservation of OmpA among the Enterobacteriaceae family. Due to its β-sheet-rich structure, OmpA forms inclusion bodies during overexpression. To mitigate this, solubilization under high-pH conditions and refolding with Lauryl dimethylamine N-oxide (LDAO) effectively preserves its native-like conformation. Semi-native SDS-PAGE and size exclusion chromatography suggest that OmpA exists as a dimer. Circular dichroism and heat modifiability analyses further confirmed its β-sheet-rich secondary structure, consistent with a β-barrel fold. However, high-resolution studies are required to confirm its oligomeric state and barrel architecture. These insights facilitate the selection of refolding processes and support investigations into the structure and function of OmpA. Functionally, in silico docking and in vitro assays revealed OmpA interaction with TLR2 from HEp-2 and Raji human B-cells. OmpA stimulation activates NFkB signaling in B-cells, leading to increased expression of proinflammatory cytokines such as TNF-α and upregulation of activation-induced cytidine deaminase (AID), a key enzyme involved in enhancing antibody diversity. Moreover, an immunoinformatic analysis has identified B-cell and T-cell epitopes within OmpA's extracellular domain, highlighting its potential as a vaccine candidate. Notably, immune simulations demonstrate that OmpA enhances both innate and adaptive immune responses. This response promotes memory cell generation and may contribute to bacterial clearance. Collectively, this study provides a foundation for future therapeutics against S. Typhimurium pathogenesis. © 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.

2026-01-01T00:00:00Z Shrivas, Sangeeta https://dspace.iiti.ac.in:8080/jspui/handle/123456789/18344 2026-05-14T12:28:26Z 2026-01-01T00:00:00Z

Title: Bioprinting taurine-incorporated gelatin methacrylate hydrogels for enhanced muscle tissue regeneration Authors: Shrivas, Sangeeta Abstract: Skeletal muscle diseases like myopathies and muscular dystrophies present significant clinical challenges with few effective treatments. To better understand disease mechanisms and accelerate therapy development, robust in vitro muscle models are needed. Extrusion- and light-based bioprinting offer precise fabrication of tissue-like constructs, but designing bioinks that support muscle cell function remains challenging. Here, we report a novel bioink in which Taurine is first methacrylated to synthesize Taurine methacrylate (TMA) enabling covalent integration into gelatin methacrylate (GelMA) networks. We systematically compared GelMA-Taurine (physical blend) versus GelMA-TMA (covalent) hydrogels, assessing mechanical stiffness, swelling behavior, and photocrosslinking kinetics. Incorporating TMA yielded improved crosslinking control, minimized overcure in DLP-printed features, and enhanced shape fidelity. SEM revealed finer pore structures and homogeneous TMA distribution, and release assays confirmed prolonged TMA retention compared to rapidly leaching Taurine. Photopatterning and 3D bioprinting of complex geometries demonstrated excellent printability of the GelMA-TMA bioink. Finally, C2C12 myoblasts encapsulated in GelMA-TMA scaffolds exhibited accelerated differentiation, increased myosin heavy chain (MyHC) expression, and more extensive myotube formation than controls. Intracellular Ca2+ imaging further demonstrated stronger receptor-mediated calcium signaling in TMA-containing constructs, suggesting improved functional maturation of C2C12-derived myotubes. Together, these results establish GelMA-TMA as a bioprintable, mechanically tunable, and biologically active platform for engineering skeletal muscle tissue in disease modeling and regenerative applications. © 2026 The Authors

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