Urea is the most widely used nitrogen fertilizer worldwide. However, ammonia volatilization, resulting from applying urea to the soil surface, causes economic and environmental losses; thus, urease inhibitors have been developed to mitigate these losses. In this work, the anti-ureolytic activity of Schiff’s base 4-(3-hydroxybenzylideneamino) phenol (3B4) and its amine-derived (3B4a) was evaluated. The most promising urease inhibitor in soil was 3B4 (55.0 ± 3.9% inhibition), with comparable results to N-(butyl) thiophosphoric triamide (p = 0.659). In the in vitro analysis (Canavalia ensiformis), the results of anti-ureolytic activity were similar, 22.6 ± 6.9% for 3B4 and 24.2 ± 9.6% for 3B4a. Biophysical interaction studies were also carried out through molecular docking studies and molecular fluorescence spectroscopy. These studies showed that both substances are preferentially competitive inhibitors, with the interaction between 3B4a and urease forming a more stable complex. In the analysis by Fourier transform infrared spectroscopy, no interaction was observed when 3B4 or 3B4a was mixed with urea (1:1) for 48 h, providing evidence of compatibility. Thus, the Schiff base 3B4 and its corresponding amine 3B4a may represent potential additives for urea fertilization aiming to assist in the urease inhibition process. worldwide However volatilization surface losses thus work antiureolytic anti ureolytic Schiffs s 43hydroxybenzylideneamino hydroxybenzylideneamino 4 3 4-(3-hydroxybenzylideneamino B (3B4 aminederived derived Ba (3B4a evaluated 3B 55.0 550 55 0 (55. 39 9 3.9 inhibition, , inhibition) Nbutyl N butyl N-(butyl p 0.659. 0659 0.659 . 659 0.659) Canavalia ensiformis, ensiformis ensiformis) similar 226 22 6 22. 69 6.9 242 24 2 24. 96 9.6 spectroscopy complex 11 1 (1:1 h compatibility Thus process (3B 55. 5 (55 3. 065 0.65 65 6. 9. (1: (5 06 0.6 (1 ( 0.

In this study, the interaction between benzothiazole (BTA, concentration of a drug required for 50% inhibition in vitro (IC50) = 0.77 mM) and benzimidazole (BIA, IC50 = 2.14 mM) with urease was quantitatively assessed, using UV-Vis, molecular fluorescence, and circular dichroism. The results showed that both compounds interact with urease by a static fluorescence quenching mechanism with a non-fluorescent complex formation. The main forces responsible for stabilizing the supramolecular complex between BTA and urease were hydrophobic while, for BIA, van der Waals interactions and hydrogen bonds were the main ones. Urease conformation changes due to the interaction process were analyzed by circular dichroism and synchronous fluorescence. Besides, a competitive assay with substrate and inhibitors was used to evaluate the preferential urease site of interaction with BTA and BIA. Our experimental and theoretical studies supported that both, BTA and BIA, are mixed-inhibitors of ureases with a slight preference to the active site of such enzymes. Finally, both BTA and BIA showed to possess anti-Helicobacter pylori (one reference strain and six clinical isolates) activity, presenting minimal inhibitory concentration (MIC) values ranging from 38-150 and 20-164 µM, respectively. The urease inhibitors omeprazole and hydroxyurea showed MIC values in the range of 46-185 µM and 1683-> 3366 µM, respectively.

ABSTRACT Passiflora edulis Sims var. flavicarpa O. Deg. (Yellow-passion fruit) is the native plant species most used by juice industries in Brazil while its leaf extracts are widely employed in folk medicine. This study evaluated the phenolic content of leaves, roots, fruit shells and pulp of plants of P. edulis in juvenile, flowering and fruiting stages. The extent of scavenging and/or degradation of reactive nitrogen and oxygen species by plant extracts was also investigated. Leaves were the organs that most accumulated phenolics/flavonoids, regardless of plant developmental stage. Leaf extracts efficiently scavenged DPPH by up to 67 % while root and fruit shell extracts effectively captured up to 80 % O2 -. Maximum activity of catalase (51.6 mmol H2O2 min-1 mg prot-1) and ascorbate peroxidase (2.2 mmol ascorbate min-1 mg prot-1) was recorded in leaf extracts from plants in the fruiting stage. Superoxide dismutase activity reached its highest levels (37.5 U min-1 mg prot-1, on average) in plant leaves of both juvenile and fruiting plants. Overall, these results suggest that, for therapeutic purposes, parts of P. edulis should be harvested when plants are in the fruiting stage due to the excellent antioxidant properties of their extracts and their accumulation of phenolic compounds.

ABSTRACT High salinity affects plants due to stimulation of osmotic stress. Cell signaling triggered by nitric oxide (NO) and hydrogen sulfide (H2S) activates a cascade of biochemical events that culminate in plant tolerance to abiotic and biotic stresses. For instance, the NO/H2S-stimulated biochemical events that occur in plants during response to high salinity include the control of reactive oxygen species, activation of antioxidant system, accumulation of osmoprotectants in cytosol, induction of K+ uptake and Na+ cell extrusion or its vacuolar compartmentation among others. This review is a compilation of what we have learned in the last 10 years about NO participation during cell signaling in response to high salinity as well as the role of H2S, a new player in the mechanism of plant tolerance to salt stress. The main sources of NO and H2S in plant cells is also discussed together with the evidence of interplay between both signaling molecules during response to stress.

The plant phenolic natural products (PNPs) protocatechuic aldehyde, syringaldehyde and vanillin were used as platforms for obtaining four urease inhibitors. Urea (urease substrate) or thiourea (urease inhibitor) core was added to the structure of newly synthesized compounds to provide inhibitors up to 230-fold more active than the PNPs they originated from. The PNP derivatives are mixed inhibitors with higher affinity to urease active site. Two compounds were as efficient as N-(butyl)thiophosphoric triamide (NBPT) toward soil. Overall, PNPs derivatives are promising urease inhibitors for use as additive in urea-based fertilizers formulations.