Waseem Ali Hasan

The NLRP3 inflammasome responds to chemically and biologically diverse stimuli, yet growing evidence indicates that this apparent diversity converges on a limited set of structural and spatial licensing steps. Here, we argue that NLRP3 regulation is best understood through an assembly‐centered framework rather than as another stimulus‐centered catalog of activators. Cryo‐electron microscopy (Cryo‐EM), biochemical, and cell‐biological studies support a model in which NLRP3 is maintained in inactive cage‐like assemblies, undergoes nucleotide‐dependent conformational rearrangements, engages NEK7, and nucleates ordered supramolecular complexes containing apoptosis‐associated speck‐like protein containing a caspase recruitment domain (ASC). We synthesize current evidence for structural licensing, interface‐level restraint, subcellular trafficking, phase‐separation‐linked organization, and post‐translational and proteostatic control of NLRP3 assembly. We then examine a less explored question with translational implications: whether peptide‐scale regulators, particularly endogenous microproteins, may control defined assembly transitions. Available evidence supports the existence of synthetic peptides that inhibit inflammasome interfaces and of endogenous microproteins that intersect with inflammatory signaling. However, direct evidence that endogenous microproteins act as dedicated interface‐mimic inhibitors of NLRP3 assembly remains lacking. This review integrates mature structural models of NLRP3 regulation with the emerging microprotein field while clearly distinguishing established mechanisms from plausible but unproven hypotheses. This perspective defines a mechanistically explicit agenda for future work, including rigorous validation of translated small open reading frames (smORFs), direct interaction mapping to defined NLRP3 surfaces, and quantitative testing of effects on assembly, signaling output, and cellular context.

| The conversion of regular pumpkin seed oil into a nanotechnology-driven composition involves encapsulating Lidocaine within the phytosome structure of the oil. This process aims to bolster its physical resilience and therapeutic advantages while mitigating potential adverse reactions. The central objective of this research centers on assessing the curative impacts of the innovative Nano phytosome pumpkin-lidocaine gel in the context of third-degree burn wound healing. The reformulation of standard pumpkin seed oil involved the encapsulation of conventional Lidocaine within a phytosome structure, resulting in the formation of nanoparticles. This modification was undertaken to enhance both the physical stability of the oil and the therapeutic properties of pumpkin seed oil, while simultaneously mitigating the potential side effects associated with Lidocaine. Evaluation of the therapeutic effect of Nano phytosome pumpkin-lidocaine gel on the healing of third burn wounds. Twenty-five,10 to 18-week- old ,white male and female adult rabbits weighting 2.5-3 kg divided to5 groups (n=5) as following negative control group, positive control group, ordinary pumpkin seed oil group, Nano phytosome pumpkin-lidocaine 100% gel group, and Nano phytosome pumpkin 100% gel group. The Nano phytosome pumpkin-lidocaine gel at a concentration of 100% and the Nano phytosome pumpkin gel at a concentration of 100% showed a significant entrapment % and loaded efficiency%, entrapment % were 95.2 ± 9.41, and 87.32 ± 8.1 respectively, while loaded efficiency% were 86.84 ± 7.77, and 79.40± 3.72 respectively. As well as, both the Nano phytosome pumpkin-lidocaine gel at a concentration of 100% and the Nano phytosome pumpkin gel at a concentration of 100% revealed a significant closure rate of 0.216±0.05, and 0.215 ±0.03 mm/day respectively, compared to ordinary pumpkin seed oil treated group, and both positive and negative control group. From this study concluded the pumpkin seed oil loaded with Nano phytosome pumpkin-lidocaine demonstrated good physical stability, reducing the crystal nature of active extract substances, with good entrapment% and loaded efficiency %, and improving the wound healing of burn wound.

Background: Research has made significant progress, with evidence indicating that enzymes that deplete amino acids may reduce the risk of various cancers. Influenza viral infections exhibit a wide host range, including birds, humans, and various other well-adapted species, and can evolve into highly pathogenic strains. The scientists sought to identify methods to mitigate this invasion, which poses a significant threat to human survival. Subjects & methods: This study focuses on the purification of L-glutaminase, a medically significant enzyme, from Bacillus subtilis. The purification process involved 70% ammonium sulfate precipitation, followed by diethylaminoethyl cellulose (DEAE-C) ion exchange chromatography and gel filtration chromatography using Sephadex G-200. From the stock solution, various concentrations (12.5, 25, and 50 μg/ml) of L-glutaminase were derived to assess their efficacy against human influenza A/Puerto Rico/8 H1N1 (IAV/PR8). The objective was to evaluate the impact of L-glutaminase on viral replication in MDCKII and A549 cells, employing plaque assays and reverse transcriptase quantitative real-time polymerase chain reaction to analyze the gene expression of specific viral proteins, including non-structural protein 1 (NS1) and nucleoprotein (NP). Results: The elution profile for L-glutaminase on the DEAE-C column revealed that the most active fractions (40-50) exhibited an enzyme activity of 200 U/mg protein and a purification fold of 21. The enzyme's specific activity at this stage was 12.5 U/mg, yielding a purification fold of approximately 8.3 and a 50% recovery of the enzyme. Results: Our findings indicated a significant decrease in the ability of IAV/PR8 to grow and replicate in MDCKII cells at multiplicities of infection (MOI) of both 0.1 and 0.01. At MOI of 0.01, plaque-forming units (PFU) per milliliter significantly decreased at concentrations of 25 and 50 μg/ml after 24 hours. Similarly, the expression of NP and NS1 proteins of IAV/PR8 was markedly downregulated at concentrations of 25 and 50 μg/ml but 8 hours. In conclusion, L-glutaminase demonstrated antiviral efficacy against the replication of IAV/PR8, likely due to its influence on the production of viral proteins NP and NS1, which are crucial for viral protein synthesis.