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Ensuring safe drinking water remains a significant challenge due to the prevalence of waterborne diseases. While chlorine-based and UV-based methods effectively kill pathogens, they often generate harmful byproducts. Consequently, there's a pressing need for innovative techniques, such as utilizing silver nanoparticles(AgNPs) renowned for their antibacterial properties. In this study, a chemical reduction technique was employed to synthesize AgNPs. Subsequently, these AgNPs underwent comprehensive characterization using techniques such as FTIR, XRD,TGA and XPS. The synthesized nanoparticles were then applied for disinfecting spring water. The experimental design was meticulously planned using the central composite design method (CCD) from Response Surface Methodology (RSM), facilitated by Design Expert software. Three key factors: AgNPs, pH, and contact time were varied across three levels, resulting in a total of 20 designed experiments. These experiments were conducted in accordance with the specified run order, culminating in the achievement of maximum bacteria growth inhibition efficiency of 99.72 % at the optimal conditions of 0.01 mg/100 mL AgNPs dose, a pH of 6, and a contact time of 20 min. Overall, the findings of this study underscore the efficiency of AgNPs in disinfecting spring water.

This study aimed to determine the effectiveness of Spathodea Campanulata derived activated carbon in removing methylene blue (MB) from wastewater. The activated carbon was prepared through chemical impregnation with H3PO4 and thermal activation at 500 °C for 2 h. The adsorption experiments were optimized using 24 full factorial designs, considering pH, contact time, initial MB concentration, and adsorbent dosage as parameters. The characterization of the activated carbon revealed favorable properties, including multiple surface functional groups, a maximum specific surface area of 1054 m2/g, and a highly porous surface morphology. The optimized conditions achieved a maximum removal efficiency of 99.95%, with pH 9, a contact time of 120 min, a dye concentration of 90 mg/L, and an adsorbent dosage of 0.2 g/100 mL being the most effective parameters. The Freundlich isotherm model provided the best fit to the experimental data, indicating a heterogeneous and multilayer adsorbent surface. The kinetics study indicated that chemisorption was the primary mechanism. In conclusion, the study indicated that Spathodea Campanulata based activated carbon could serve as a cost-effective adsorbent for removing MB from aqueous solutions

The arylsulfatase A (ARSA) gene is observed to be deficient in patients with metachromatic leukodystrophy (MLD), a type of lysosomal storage disease. MLD is a severe neurodegenerative disorder characterized by an autosomal recessive inheritance pattern. This study aimed to map the most deleterious mutations at the metal binding sites of ARSA and the amino acids in proximity to the mutated positions. We utilized an array of computational tools, including PredictSNP, MAPP, PhD-SNP, PolyPhen-1, PolyPhen-2, SIFT, SNAP, and ConSurf, to identify the most detrimental mutations potentially implicated in MLD collected from UniProt, ClinVar, and HGMD. Two mutations, D29N and D30H, as being extremely deleterious based on assessments of pathogenicity, conservation, biophysical characteristics, and stability analysis. The D29 and D30 are located at the metal-interacting regions of ARSA and found to undergo post-translational modification, specifically phosphorylation. Henceforth, the in-depth effect of metal binding upon mutation was examined using molecular dynamics simulations (MDS) before and after phosphorylation. The MDS results exhibited high deviation for the D29N and D30H mutations in comparison to the native, and the same was confirmed by significant residue fluctuation and reduced compactness. These structural alterations suggest that such mutations may influence protein functionality, offering potential avenues for personalized therapeutic and providing a basis for potential mutation-specific treatments for severe MLD patients., (Copyright © 2024. Published by Elsevier Inc.)

Blau syndrome (BS), which affects the eyes, skin, and joints, is an autosomal dominant genetic inflammatory disorder. BS is caused by mutations in the NOD2 gene. However, there are no direct treatments, and treatment with conventional anti-inflammatory drugs such as adrenal glucocorticoids, anti-metabolites, and biological agents such as anti-TNF and infliximab have all been attempted with varying degrees of success. In this study, we tried to identify all the reported mutations in the NOD2 protein that cause BS. Collectively, 114 missense mutations were extracted from the UniProt, ClinVar, and HGMD databases. The mutations were further subjected to pathogenic, stability, and conservation analyses. According to these computational analyses, six missense mutations (R334Q, R334W, E383G, E383K, R426H, and T605P) were found to be highly deleterious, destabilizing, and positioned in the conserved position. ADP to ATP conversion plays a crucial role in switching the closed-form of NOD2 protein to the open-form, thus activating the protein. Accordingly, the mutations in the ADP binding sites have received more attention in comparison to the mutations in the non-ADP binding positions. Interestingly, the W490L mutation is positioned in the ADP binding site and exhibits highly deleterious and destabilizing properties. Additionally, W490L was also found to be conserved, with a ConSurf score of 7. Therefore, we further performed homology modeling to determine the 3D structure of native NOD2 and the W490L mutant. Molecular docking analysis was carried out to understand the change in the interaction of ADP with the NOD2 protein. We observed that ADP had a stronger interaction with the native NOD2 protein compared to the W490L mutant. Finally, ADP complexed with native NOD2 and W490L mutant were subjected to molecular dynamics simulations, and the trajectories were analyzed. In the simulations, we observed decreased deviation and fluctuations in native NOD2, whereas decreased compactness and inter- and intramolecular hydrogen bonds were observed in the W490L mutant. This study is expected to serve as a platform for developing targeted drug therapy for BS., (Copyright © 2020 Elsevier Inc. All rights reserved.)

The G2019S substitution in the Leucine-rich repeat kinase 2 (LRRK2) is significantly associated with Parkinson's disease (PD). This substitution was identified in both familial and sporadic forms of PD with a higher frequency. Few computational studies have reported the impact of G2019S substitution on inhibitors of the kinase domain of LRRK2. However, no computational study deeply investigated the possible impact of the G2019S substitution on the kinase domain in its Apo conformation. Therefore, in this study, we used 200 ns molecular dynamic simulation using the GROMACS 5.1.4 package software to investigate the impact of the G2019S substitution on the structure of the kinase domain of LRRK2. Our results indicate that the G2019S substitution affects the dynamics and stability of LRRK2 by decreasing the flexibility and increasing the compactness of the kinase domain and showing its tendency to be in an active conformation for long time interval because of the high energy barrier between active and inactive conformation. This study predicts the molecular pathogenicity mechanism of the G2019S on patients with PD and provides a potential platform for developing therapeutics for patients with PD that harbor this amino acid substitution., (Copyright © 2019 Elsevier Ltd. All rights reserved.)