https://dspace.nii.res.in//https://dspace.nii.res.in/handle/123456789/7 2026-04-03T13:38:29Z 2026-04-03T13:38:29Z Dalal, N Dhiman, TK Lakshmi, GBVS Singh, AK Solanki, PR Kumar, A https://dspace.nii.res.in//https://dspace.nii.res.in/handle/123456789/1630 2025-07-18T05:28:45Z 2022-01-01T00:00:00Z

Title: MIP based sensor for detection of gut microbiota-derived Indoxyl Sulfate using PANI- Graphene-NiS2. Authors: Dalal, N; Dhiman, TK; Lakshmi, GBVS; Singh, AK; Solanki, PR; Kumar, A Abstract: Indoxyl sulphate (IS) is a gut microbiota-derived metabolite that is involved in human health and dis- eases. The normal range of IS in human serum may be in the range of 0.024e0.05 mg/dl, but the altered IS level has been observed in diseased conditions, such as chronic kidney diseases, diabetes and cancer, which implicate IS as a diagnostic and prognostic biomarker. In the current work, a molecularly imprinted polymer (MIP)-based electrochemical sensor was made for the quantification of IS in a wide concentration range. The IS sensing was studied using DPV, revealing decreasing peak current with increasing IS concentrations. The MIP/ITO electrode has shown a good response from 1.0 pM to 6.0 mM which is linear in trend, with a sensitivity of 0.0362 mA (log (ng/mL)) -1 cm -2 and a lower limit of detection of 0.286 pg/mL and a low response time of 5 min. The interference study also confirmed the specificity of MIP-based electrochemical sensor toward IS detection. The real sample study confirmed the MIP-based sensor's applicability to detect IS in urine samples. The sensitive, cheap, and reproducible MIP-based detection of IS may offer a new diagnostic approach to diagnose various diseases implicated with altered level of IS in human serum and urine.

2022-01-01T00:00:00Z Arora, Ashish Dasgupta, Arunava Biswal, Bichitra Kumar Jain, Anupam Tripathi, Sarita Pal, Ravi Kant Singh, Shriya Zohib, Muhammad Yadav, Vikash https://dspace.nii.res.in//https://dspace.nii.res.in/handle/123456789/1629 2025-07-10T12:14:13Z 2025-01-01T00:00:00Z

Title: Structural and biophysical characterization of PadR family protein Rv1176c of Mycobacterium tuberculosis H37Rv Authors: Arora, Ashish; Dasgupta, Arunava; Biswal, Bichitra Kumar; Jain, Anupam; Tripathi, Sarita; Pal, Ravi Kant; Singh, Shriya; Zohib, Muhammad; Yadav, Vikash Abstract: Rv1176c of Mycobacterium tuberculosis H37Rv belongs to the PadR-s1 subfamily of the PadR family of protein. Rv1176c forms a stable dimer in solution. Its stability is characterized by a thermal melting transition temperature (Tm) of 39.4 °C. The crystal structure of Rv1176c was determined at a resolution of 2.94 Å, with two monomers in the asymmetric unit. Each monomer has a characteristic N-terminal winged-helix-turn-helix DNA-binding domain. Rv1176c C-terminal is a coiled-coil dimerization domain formed of α-helices α5 to α7. In the Rv1176c dimer, there is domain-swapping of the C-terminal domain in comparison to other PadR homologs. In the dimer, there is a long inter-subunit tunnel in which different ligands can bind. Rv1176c was found to bind to the promoter region of its own gene with high specificity. M. smegmatis MC2 155 genome lacks homolog of Rv1176c. Therefore, it was used as a surrogate to characterize the functional role of Rv1176c. Expression of Rv1176c in M. smegmatis MC2 155 cells imparted enhanced tolerance towards oxidative stress. Rv1176c expressing M. smegmatis MC2 155 cells exhibited enhanced intracellular survival in J774A.1 murine macrophage cells. Overall, our studies demonstrate Rv1176c to be a PadR-s1 subfamily transcription factor that can moderate the effect of oxidative stress.

2025-01-01T00:00:00Z Kumar, Raj Kumari, Pratibha Gaurav, Neelanshu Kumar, Ravi Singh, Darshana Malhotra, Poonam Singh, Shravan Kumar Bhatta, Rabi Sankar Kumar, Anil Nagarajan, Perumal Singh, Surender Dalal, Nishu Roy, Bal Gangadhar Bhatt, Anant Narayan Chandna, Sudhir https://dspace.nii.res.in//https://dspace.nii.res.in/handle/123456789/1586 2025-08-12T04:36:56Z 2025-01-01T00:00:00Z

Title: N-acetyl-L-tryptophan provides radioprotection to mouse and primate models by antagonizing the TRPV1 receptor and substance P inhibition. Authors: Kumar, Raj; Kumari, Pratibha; Gaurav, Neelanshu; Kumar, Ravi; Singh, Darshana; Malhotra, Poonam; Singh, Shravan Kumar; Bhatta, Rabi Sankar; Kumar, Anil; Nagarajan, Perumal; Singh, Surender; Dalal, Nishu; Roy, Bal Gangadhar; Bhatt, Anant Narayan; Chandna, Sudhir Abstract: Purpose: The present study was carried out to evaluate the radioprotective activities of N-acetyl-L-tryptophan (L-NAT) using rodent and non-human primate (NHP) models. Materials and methods: The antagonistic effect of L-NAT on the Transient receptor potential vanilloid-1 (TRPV1) receptor and substance P inhibition was determined using molecular docking and Elisa assays. The in vivo radioprotective activity of L-NAT was evaluated using whole-body survival assays in mice and NHPs. Radioprotective activity of L-NAT was also determined at the systemic level using quantitative histological analysis of bone marrow, jejunum, and seminiferous tubules of irradiated mice. Results: Molecular docking studies revealed a strong binding of L-NAT with TRPV1 receptor at similar binding pockets to which capsaicin, an agonist of the TRPV1 receptor, binds. Further, capsaicin and gamma radiation were found to induce substance P levels in the intestines and serum of the mice, while L-NAT pretreatment was found to inhibit it. Significant whole-body survival (>80%) was observed in irradiated (9.0 Gy) mice that pretreated with L-NAT (150 mg/kg, b.wt. im) compared to 0% survival in irradiated mice that not pretreated with L-NAT. The quantitative histology of the hematopoietic, gastrointestinal, and male reproductive systems demonstrated significant protection against radiation-induced cellular degeneration. Interestingly, 100% survival was observed with irradiated NHPs (6.5 Gy) that pretreated with L-NAT (37.5 mg/kg, b.wt.im). Significant improvement in the hematology profile was observed after days 10-20 post-treatment periods in irradiated (6.5 Gy) NHPs that were pretreated with L-NAT. Conclusion: L-NAT demonstrated excellent radioprotective activity in the mice and NHP models, probably by antagonizing TRPV1 receptor and subsequently inhibiting substance P expression.

2025-01-01T00:00:00Z Kumar, Anil Gulati, Payal Lakshmi, Gbvs Mohan, Anand Sharma, Geeta Raj Solanki, Pratima R Verma, Awadhesh Kumar https://dspace.nii.res.in//https://dspace.nii.res.in/handle/123456789/1585 2025-07-10T11:42:56Z 2025-01-01T00:00:00Z

Title: Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) Authors: Kumar, Anil; Gulati, Payal; Lakshmi, Gbvs; Mohan, Anand; Sharma, Geeta Raj; Solanki, Pratima R; Verma, Awadhesh Kumar Abstract: Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact of TMAO on disease mechanisms. However, detailed insights into the interaction mechanisms, preferred binding locations, and conformational changes in BSA upon binding TMAO are still unclear. TMAO interacts with serum albumin in human body and thus, a model study of interaction for TMAO-BSA conjugate is presented in support of it. Decrease in absorbance intensity of protein upon interaction with metabolites reveals conjugate formation, while fluorescence spectroscopy indicate static quenching. Contact angle measurements further reveal the hydrophilic nature of the TMAO-BSA complex, while CD and FTIR support conformational changes in BSA upon binding but structure remain intact. Computational studies, such as molecular docking, molecular dynamics simulation and, MM/GBSA, confirm a stable complex with a binding energy of - 3.6 kcal/mol. These findings provide a foundation for understanding the pharmacodynamics and pharmacokinetics of TMAO and may aid in developing strategies for treating diseases, such as chronic kidney disease and neurological disorder where TMAO-serum albumins interaction are implicated.

2025-01-01T00:00:00Z