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Durum wheat, less immunogenically intolerant than bread wheat, originates from diploid progenitors known for nutritional quality and stress tolerance. Present study involves the analysis of major grain parameters, viz. size, weight, sugar, starch, and protein content of Triticum durum (AABB genome) and its diploid progenitors, Triticum monococcum (AA genome) and Aegilops speltoides (BB genome). Samples were collected during 2–5 weeks after anthesis (WAA), and at maturity. The investigation revealed that T. durum displayed the maximum grain size and weight. Expression analysis of Grain Weight 2 (GW2) and Glutamine Synthase (GS2), negative and positive regulators of grain weight and size, respectively, revealed higher GW2 expression in Ae. speltoides and higher GS2 expression in T. durum. Further we explored total starch, sugar and protein content, observing higher levels of starch and sugar in durum wheat while AA genome species exhibited higher protein content dominated by the fractions of albumin/globulin. HPLC profiling revealed unique sub-fractions in all three genome species. Additionally, a comparative transcriptome analysis also corroborated with the starch and protein content in the grains. This study provides valuable insights into the genetic and biochemical distinctions among durum wheat and its diploid progenitors, offering a foundation for their nutritional composition. [ABSTRACT FROM AUTHOR]

Pectin-crosslinked gum ghatti hydrogel (PGH) has been synthesized utilizing pectin and gum ghatti through an uncomplicated and inexpensive copolymerization method. X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM-elemental mapping), Brunauer-Emmett-Teller (BET), and X-ray photoelectron spectroscopy (XPS) characterization techniques have been employed to determine various structural, chemical and compositional characteristics of fabricated PGH. Three different weight ratios (1:1, 2:1, or 1:2 for pectin and gum ghatti, respectively) were employed to synthesize three distinct types of PGH. Swelling studies has been done to determine the best ratios for PGH fabrication. PGH has been assessed as an adsorbent for the removal of malachite green dye from aqueous solutions. The effects of PGH dosage (100–400 mg/L), dye concentration (10–160 mg/L), pH (2–9 pH), adsorption time (0–480 min), and temperature (25–55 °C) has been examined through batch solutions. According to Langmuir isotherm analysis, the maximum adsorption capacity is 658.1 mg/g. By using pseudo-second-order kinetics and the Freundlich adsorption isotherm, the adsorption process could be well explained. After five consecutive cycles, PGH had an adsorption percentage of 86.917 % for the malachite green dye. It is safe for the environment and may be used to remove malachite green (MG) dye from aqueous solutions. [Display omitted] • Pectin-crosslinked gum ghatti hydrogel (PGH) synthesis using copolymerization • Study of physicochemical properties of PGH • PGH effectively adsorbed malachite green (MG) dye. • Showing a maximum capacity of 658.1 mg/g according to Langmuir isotherm analysis • Freundlich isotherm model fits well, indicating a heterogeneous adsorption process. [ABSTRACT FROM AUTHOR]

Acinetobacter baumannii is a notorious pathogen that commonly thrives in hospital environments and is responsible for numerous nosocomial infections in humans. The burgeoning multi-drug resistance leaves relatively minimal options for treating the bacterial infection, posing a significant problem and prompting the identification of new approaches for tackling the same. This motivated us to focus on non-canonical nucleic acid structures, mainly G-quadruplexes, as drug targets. G-quadruplexes have recently been gaining attention due to their involvement in multiple bacterial and viral pathogenesis. Herein, we sought to explore conserved putative G-quadruplex motifs in A. baumannii. In silico analysis revealed the presence of eight conserved motifs in genes involved in bacterial survival and pathogenesis. The biophysical and biomolecular analysis confirmed stable G-quadruplex formation by the motifs and showed a high binding affinity with the well-reported G-quadruplex binding ligand, BRACO-19. BRACO-19 exposure also decreased the growth of bacteria and downregulated the expression of G-quadruplex-harboring genes. The biofilm-forming ability of the bacteria was also affected by BRACO-19 addition. Taking all these observations into account, we have shown here for the first time the potential of G-quadruplex structures as a promising drug target in Acinetobacter baumannii , for addressing the challenges posed by this infamous pathogen. [ABSTRACT FROM AUTHOR]

Heart failure (HF) is emerging as a leading cause of death worldwide. Estimation of BNP levels is a routine diagnosis in these patients. However, in patients having high body-mass index (BMI), renal disease or in geriatric patients, BNP level is reported to be noisy and leads to incongruous conclusion. Thus, for better risk stratification among heart failure patients, it is imperative to look for a superior biomarker. In recent times, sST2 has shown promise as a biomarker. Identifying such biomarkers in peripheral blood of HF patients, need an affine and selective molecular recognition element. Thus, in the current study an aptamer (sS9_P) against sST2 was identified from an aptamer library. Systematic Evolution of Ligands through Exponential enrichment (SELEX) derived aptamer evinced role of its primer binding domains in maintaining its selectivity. This aptamer candidate demonstrated dissociation constant (Kd) in low nanomolar range, and the Limit of Detection (LOD) was ~4 ng. Circular dichroism confirms the formation of complex stem-loop like structure. The well characterized sS9_P aptamer was used in an Aptamer Linked Immobilized Sorbent Assay (ALISA) to detect sST2 level in patients' serum (n = 99). Aptamer sS9_P has shown significant discrimination to differentiate HF patients and healthy volunteers with a reasonable specificity (~83 %) with a modest sensitivity of ~64 %. While sST-2 antibody has shown poor specificity of ~44% but good sensitivity (~87%). The insight obtained from this study indicates that a combination of aptamer and antibody-based assay can be used to design a point-of-care assay for the rapid detection of HF patients in emergency settings. [ABSTRACT FROM AUTHOR]