Alzahra University

Chenopodium quinoa is an emerging halophyte plant that has gained significant attention from researchers in recent years due to its high nutritional value and resilience to environmental stress. This plant serves as an excellent substitute for rice and wheat. However, there has been limited research on it, leaving many of its genes still unidentified. The objective of this research was to identify gene patterns and conduct a bioinformatics analysis across various fields. The expression sequence of the betaine aldehyde dehydrogenase (BADH) gene was predicted using bioinformatics software such as PlantCARE and PlantPan. The findings indicated that different cultivars provide valuable information regarding resistance to the binding sites of MYB transcription factors, hormone response regions, and both promoter and enhancer regions, which contain 32 cis-regulatory elements. This emphasized the role of the BADH gene in responding to abiotic stress. Additionally, the research revealed that the BADH gene activates oxidoreductase activity across different cultivars, influencing NAD or NADP receptors that contribute to stress resistance. The protein lengths identified were 454 and 500 amino acids, respectively. Chloroplast analysis revealed that the GC content for the BADH gene was 37%. From this analysis, it was determined that out of 128 distinct functional genes in the genome, approximately 84 are protein-coding genes. An examination of the domains and motifs in the target genes showed that they contain two conserved sequences: Aldedh and DUF1487. Furthermore, miRNA analysis and promoter investigations indicated that the BADH gene plays a vital role in activating processes related to arginase, protein kinases, superoxide dismutase, tubulins, and membrane proteins. The gene is also crucial for activating nuclear transcription factors through receptor activation. In conclusion, the results suggest that BADH genes contribute to the plant's resistance to salt stress through various mechanisms. Stress acts as a trigger for the activation of this gene, effectively safeguarding the plant against the detrimental effects of environmental stresses.

In this study, we designed an efficient siRNA for PKMYT1 gene knockdown and evaluated the binding affinity of various natural small molecules to key proteins associated with breast cancer through molecular docking and molecular dynamics (MD) simulations. Subsequently, among these molecules, The small molecule, SCHEMBL7562664, was introduced as a "golden ligand" that showed potent multi-target activity as an antagonist for aromatase, estrogen receptor α, HER2, and PARP10, and as an agonist for MT2 and STING. Next, MD simulations of six protein- golden ligand complexes (PDB IDs: 4QXQ, 5GS4, 5JL6, 5LX6, 6ME6, and 7PCD), performed with GROMACS over 100 ns at 298.15 K, provided valuable information about their structural dynamics. Analysis of the radius of gyration (Rg) revealed that, while five complexes (7PCD, 5GS4, 5LX6, 4QXQ, and 5JL6) maintained compact structures (Rg between 1.7 and 2.3 nm), the 6ME6 complex exhibited a more extended and flexible conformation (average Rg ∼3.4 nm). Complementary RMSD analysis confirmed that most complexes rapidly stabilized with minimal deviations (generally <0.3 nm), whereas the 6ME6 complex showed higher variability, reaching up to 0.67 nm. Furthermore, Binding free energy calculations using MM-GBSA and PBSA methods further supported these findings, with energies ranging from -21.45 ± 2.28 kcal/mol (5LX6) to -39.79 ± 1.34 kcal/mol (6ME6), indicating an optimal balance between intrinsic interactions and desolvation costs in the 6ME6 and 5JL6 systems. Based on DFT results, the golden ligand showed higher stability and lower reactivity compared to control ligands such as aromatase, tamoxifen, and dacomitinib, potentially leading to reduced off-target interactions and a more favorable safety profile. The integration of these data underscores the therapeutic potential of SCHEMBL7562664 as a multi-target agent for breast cancer, with promising pharmacokinetic properties that can be optimized for local treatment by incorporation into a 3D scaffold.

An efficient nano-catalyst based on melamine-terephthalaldehyde framework with ionic liquid functionality (MTF-IL) was synthesized through the post-synthetic modification of organic linkers with 1-methylimidazolium bromide.This MTF-IL was investigated for its efficacy as a metal-free nano-catalyst in fructose dehydration to synthesize 5-hydroxymethylfurfural (HMF).Optimization via Response Surface Methodol. (RSM) identified optimal reaction conditions of 21 wt% catalyst, 100 °C, and 50 min, resulting in a remarkable HMF yield of 98 % in DMSO.Kinetic studies suggested that the dehydration process mediated by MTF-IL follows pseudo-first-order kinetics, exhibiting a low activation energy of 14 kJ. mol^-1 at optimal conditions.The nature of the anion pair in MTF-IL significantly influenced its catalytic activity, with enhanced performance corresponding to bromide.Addnl., MTF-IL demonstrated characteristics of a heterogeneous catalyst, facilitating straightforward recovery and reuse.This research underscores the potential of covalent organic framework-derived solid acid catalysts for the valorization of biomass carbohydrates.