RESUMO
The occurrence of arsenic in the surroundings raises apprehension because its detrimental impacts on both human health and the ecology. Since adsorption is an effective, affordable method that can be adjusted to specific environmental circumstances, it is a sustainable solution for the removal of arsenic from the aquatic environment. Utilizing biomass that has been chemically activated may be a viable way to increase the adsorption capacity of the material, reduce arsenic pollution, and protect the environment and human health. In the proposed research, Fe(III) loaded saponified Punica granatum peel (Fe(III)-SPGP) has been synthesized to remove arsenic from aqueous solutions. FTIR and SEM analysis were utilized to carry out the characterization of the biosorbents. Batch experiments were carried out by altering several factors including pH and contact time, in addition to initial concentration and desorption. The most effective pH for As(III) adsorption using Fe(III)-SPGP was discovered to be 9.0. After determining that a pseudo-second-order kinetic model was the one that provided the greatest fit for the results of the experiment, the model developed by Langmuir was applied. It was discovered that the maximum adsorption of As(III) that could be adsorbed by Fe(III)-SPGP was 63.29 mg/g. The spent biosorbent may easily be reused again in subsequent applications. Based on these findings, Fe(III)-SPGP shows promise as a cheap effective sorbent for excising contaminants of As(III).
RESUMO
A bioassay-guided isolation on the plant Zanthoxylum armatum DC yielded compounds tambulin (1), and prudomestin (2), from ethyl acetate fraction which showed the highest ROS inhibiting activity (IC50 = 17.8 ± 1.1 µg/mL). Structure elucidation of pure compounds was done using mass and NMR spectroscopic techniques. Compounds 1 and 2 revealed potent ROS inhibition with IC50 = 7.5 ± 0.3 and 1.5 ± 0.3 µg/mL, respectively, as compared to standard ibuprofen (IC50 = 11.2 ± 1.9 µg/mL). Likewise, both compounds 1 and 2 showed potent antioxidant activity with IC50 = 32.65 ± 0.31 and 26.96 ± 0.19 µg/mL, respectively. In vitro studies were supported by molecular docking and drug-likeliness properties. In silico studies of 1 and 2 with cyclooxygenase-2 (COX-2) showed perfect binding affinity with binding energies of -8.4 and -8.6 kcal/mol, respectively, comparable to standard ibuprofen (-7.7 kcal/mol). Drug likeness and ADMET showed higher gastrointestinal absorption of 1 and 2 and no toxic impact.
RESUMO
Tambulin, a flavonol isolated from Zanthoxylum armatum, showed potent insulin secretory activity in our preliminary anti-diabetic screening. Here, we explored the insulin secretory mechanism(s) of tambulin focusing in glucose-dependent, KATP â and Ca2+âchannels dependent, and cAMP-PKA pathways. Mice islets and MIN6 cells were incubated with tambulin in the presence of pharmacological agonists/antagonists and the secreted insulin was measured using mouse insulin ELISA kit. The intracellular cAMP was measured by an acetylation cAMP ELISA kit. Tambulin (200⯵M) showed potent insulin secretory activity only at stimulatory glucose (11-25â¯mM) concentrations; however, no change in insulin release was observed at basal glucose both in mice islets and MIN6 cells. Notably, in the presence of diazoxide, a KATP channel opener; the incomplete inhibition of tambulin-induced insulin secretion was observed whereas, complete inhibition was found using verapamil, an L-type Ca2+ channel blocker. Furthermore, the insulinotropic potential of tambulin was amplified in tolbutamide treated, and depolarized islets suggest tambulin's target other than tolbutamide. Tambulin showed no additive effect in the IBMX-induced intracellular cAMP; whereas, exerted an additive effect in the IBMX-induced insulin secretion. Furthermore, tambulin-induced insulin secretion was dramatically inhibited by PKA inhibitor (H-89), while moderate inhibition was found by using PKC inhibitor (calphostin C). Molecular docking studies also showed the best binding affinities of tambulin with PKA suggest the PKA dependent signaling cascade is involved more in tambulin-induced insulin secretion. Based on these findings, it is concluded that tambulin stimulates insulin secretion in a Ca2+ channel-dependent but KATP channel-independent manner, most likely by activating the cAMP-PKA pathway.