Determination of biological activities of malabar spinach (Basellaalba) fruit extracts and molecular docking against COX-II enzyme.

To achieve the health benefit from the natural of Basella. Albafruit. This study intended to figure out the bioactive compounds in the two varieties of B. alba (native and hybrid) fruit extract and measurement its biological activities like antioxidant, anti-inflammatory, cytotoxic activities and a molecular docking were performed to observed the pharmaceutical impact on the anti-inflammatory Cyclooxygenase-2 (COX-2) enzyme. The cold extractions along with GC-MS were used for the extraction of and analysis of phytoconstituents from B. alba fruit. The hemolytic inhibitory and BSA (Bovine serum albumin)-denaturation assay, DPPH(2,2-diphenyl-1-picrylhydrazyl) and H2O2-free radical scavenging analysis, and brine shrimp lethalness test were performed to measure the biological activities of the extracted The biological activities assay results showed that the ethanol extract of native malabar spinach exhibited dose-dependent antioxidant activity. The IC50 value 21.55 ± 1.51 µg/mL was for DPPH scavenging assay and 23.36 ± 0.36 µg/mL was for H2O2 scavenging analysis. In anti-inflammatory activity assessment study, the IC50 values of the ethanol extracts were 20.52 ± 0.91 µg/mL for BSA inhibition and 20.43 ± 1.30 µg/mL for RBC hemolytic inhibitory study. In this study, cytotoxicity test results reveal that aqueous extract exhibited no cytotoxicity as compared to ethanol and ethyl acetate extract (LD50 = 875.27 µg/mL). Conversely, the current study insist the in silico analysis, to find out the anti-inflammatory activity of the investigated two fruit varieties due to pharmacokinetics analysis, toxicity properties analysis, ADMETand molecular docking. The result of this study signified that both (native and hybrid) malabar spinach fruit varieties contain phytoconstituents with potent antioxidant, anti-inflammatory, and cytotoxic action.Moreover, the in vitro and in silico results suggest that the native and hybrid fruit varieties of the extracts could be a superior striver for future appraisal as a prospective therapeutically active ingredient.

Development of a bionanotechnological phosphate removal system with thermostable ferritin.

Phosphate removal to ecologically desired levels of <0.01 mg/L is currently dependent on large overdosing of metal salts and production of large amounts of chemical sludge. The present study focuses on the development and performance of a new bionanotechnological phosphate removal system, based on sorption of oxoanions by nanoscale ferric iron particles stabilized within thermostable ferritin from the hyperthermophilic archaeon Pyrococcus furiosus (PfFrt). Laboratory studies show that this thermostable protein nanocage has fast kinetics for phosphate uptake at very low concentrations by catalytic oxidation of iron. In this study we demonstrate essentially complete phosphate removal with a capacity of approximately 11 mg/g PfFrt. Ferritin can easily be immobilized and is amenable to fast and efficient regeneration, making recovery of phosphate possible. The phosphate removal process with PfFrt is, due to its high affinity, able to reach ecologically desired phosphate levels and in addition it is cost competitive with existing techniques.

Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization.

Pyrococcus furiosus ferredoxin is a small metalloprotein that shuttles electrons between redox enzymes. In its native 4Fe-4S form the protein is highly thermostable. In addition to three cluster-ligating cysteines, two surface cysteine residues (C21 and C48) are present. We used the reactivity of these surface thiols to directly immobilize ferredoxin on a bare gold electrode, with an orientation in which the cluster is exposed to solution. Voltammetry, X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM) studies established the immobilization of the 4Fe form. Native and recombinant wild-type ferredoxins were compared with the C48S, C21S, and C21S/C48S mutants. The variants with one and two surface cysteines can be directly chemisorbed on bare gold. Cyclic voltammetry demonstrated that the reduction potentials are similar to those in solution. The interfacial electron transfer kinetics revealed that the reduction is gated by the interconversion between two oxidized species. AFM images showed that dimers are chemisorbed at low ionic strength, while monomers are present at high ionic strength. XPS spectra revealed the presence of S, Fe, C, N, and O at the surface, which are assigned to the corresponding atoms in the peptide and the cofactor. Analysis of the sulfur spectrum corroborates that both C21 and C48 form gold-thiolate bonds. Moreover, two inorganic sulfide and two iron species were identified, suggesting an inhomogeneous charge distribution in the 4Fe-4S cluster. In conclusion, P. furiosus ferredoxin can be directly and vectorially chemisorbed on gold with retention of its properties. This may provide a biocompatible electrode surface with docking sites for redox enzymes.