Lanthanide Chlorides Decrease the Antioxidant Property of Human Serum Albumin

Substantial conformational changes of human serum albumin, HSA, induced by Lanthanide chlorides (Ce3+, La3+, Er3+) in phosphate buffer, 10 mmol L-1 at pH 7.4, was studied by Isothermal Titration Calorimetry, ITC. The strong negative cooperativity of Lanthanide chlorides interaction with HSA recovered from the extended solvation model, indicates that HSA denatures as a result of its interaction with toxic Lanthanide chlorides. DOI: http://dx.doi.org/10.17807/orbital.v9i1.94

Removal of Reactive Red 74 Dye from Textile Industrial Waste using Zinc Oxide Nanoparticle

Global population growth and industrial activities in recent decades has been caused to enter excessive amount of pollutants to water resources. Industrial textile dyes are an important class of the pollutants in the sewage system. Disposal of the dyes in precious water resources must be avoided, however, and for that various treatment technologies are in use. Considering the toxicity of the pollutants, their removal from water resources is necessary. In this research, removal of reactive red 74, RR47, from aqueous solution by zinc oxide nanoparticles was investigated and the affecting parameters such as pH, contact time and adsorbent mass on removal efficiency were determined. Langmuir and Freundlich isotherms were studied and the results indicated that the adsorption process obey the Langmuir and Freundlich isotherms. The experimental results also showed that the pseudo-second order kinetic equation could nicely describe the sorption kinetics

Thermodynamic Study of Comfarol Binding to Urease

Isothermal Titration Calorimetry, ITC, was used to study of Jack Bean urease, JBU, binding with comfarol in phosphate buffer at pH 7.4. Data analyzing of comfarol interaction with JBU was performed by the extended solvation model and the positive cooperativity of comfarol with JBU indicates that comfarol causes stabilization of the JBU structure. DOI: http://dx.doi.org/10.17807/orbital.v11i3.136

Thermodynamic Study of Comfarol Binding to Urease

Isothermal Titration Calorimetry, ITC, was used to study of Jack Bean urease, JBU, binding with comfarol in phosphate buffer at pH 7.4. Data analyzing of comfarol interaction with JBU was performed by the extended solvation model and the positive cooperativity of comfarol with JBU indicates that comfarol causes stabilization of the JBU structure. DOI: http://dx.doi.org/10.17807/orbital.v11i3.136

Study of jack bean urease interaction with luteolin by the extended solvation model and docking simulation

Abstract: In this study, the interaction between Luteolin and urease was made at 300 K in aqueous buffer solutions using isothermal titration calorimetry. The extended solvation model was used to calculate the solvation parameters. Moreover, to determine the interaction of Luteolin with Jack Bean Urease (JBU), a molecular docking process was performed. The purpose of this investigation was to measure the inhibitory effects of Luteolin on the activity and structure of urease. Molecular docking analysis confirmed the extended solvation model

A New Insight Into the Anti Proliferative and Apoptotic Effects of Fulvic and Humic Acids as Bio Product of Humus on Breast Cancer Cells, Optimized by Response Surface Methodology

Today, plant compounds and substances of natural origin as bio products are strongly recommended for the prevention and treatment of cancer. In the field of biomedicine antiviral, anti-inflammatory, anti-oxidant properties among the most known activities of Humus and the products obtained from humus. In this study, the effect of humic and fulvic acids (HA, FA), bio product of humus, on breast cancer cells (MCF7), the most common cancer among women, was investigated. To achieve optimum cytotoxic time and determine the effect of the different parameters the Response Surface Methodology (RSM) was applied. The main parameters influencing the cytotoxic performance in the MTT assay, such as time and concentrations were regarded. The cell viability was measured using different concentrations of HA and FA including 10, 50, 100, and 200 µg/mL for 14, 24, and 48 h, respectively. Apoptosis, cell cycle, mechanical properties and survivin gene expression of MCF7 cells treated with HA and FA were analyzed after 14 h. Our results showed that HA and FA induced apoptosis, reduced cell viability and gene expression in the cured MCF7 cells. We have seen a dose-dependent behavior of HA in increasing the cell population in phase Sub-G1. The results of AFM showed that the increasing behavior of elastic modulus value and cell–cell adhesion forces were dose-dependent in cells treated with HA and FA. The golden result of this study was the matching of laboratory and statistical results which confirms the success of the RSM model in biological researches

Molecular dynamics simulations, molecular docking, and kinetics study of kaempferol interaction on Jack bean urease: Comparison of extended solvation model

Since the urease enzyme creates gastric cancer, peptic ulcer, hepatic coma, and urinary stones in millions of people worldwide, it is essential to find strong inhibitors to help patients. Natural products are well known for their beneficial effects on health and efforts are being made to isolate the ingredients, the so-called flavonoids. Flavonoids are now considered as an indispensable component in a variety of nutraceutical, pharmaceutical, and cosmetic applications. Kaempferol (KPF) is an antioxidant found in many fruits and vegetables. Many reports have explained the significant effects of dietary KPF in reducing the risk of chronic diseases such as cancer, ischemia, stroke, and Parkinson’s. The current study aimed at investigating the inhibitory impact of KPF on Jack bean urease (JBU) using molecular dynamics (MD) simulations and molecular mechanics Poisson–Boltzmann surface area (MM-PBSA) calculations to confirm the results obtained from isothermal titration calorimetry (ITC), extended solvation model, and docking software. In addition, UV–VIS spectrophotometry was used to study the kinetics of urease inhibition. Calorimetric and spectrophotometric determinations of the kinetic parameters of this inhibition indicate the occurrence of a reversible and noncompetitive mode. Also, the docking and MD results indicated that the urease had well adapted to the kaempferol in the binding pocket, thereby forming a stable complex. Kaempferol displayed low binding energy during MMPBSA calculations. The inhibitory potential of kaempferol was confirmed by experimental and simulation data, but in vivo investigations are also recommended to validate our results

Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin

We have investigated the interactions between β-lactoglobulin, BLG, and new synthesized Cu(II) complex (2,2′-dibipyridine Cu(II) chloride) using isothermal titration calorimetry (ITC) methods at different temperatures of 298 and 310 K. The heats of BLG + Cu(II) interactions are reported and analyzed in terms of the extended solvation theory for calculation of binding and thermodynamic parameters of the interaction. The results suggested that binding of Cu(II) complex on BLG resulted in significant changes on the tertiary structure and conformation of protein via increasing of hydrophobicity and inducing partially unfolded structure in BLG which has a good agreement with the solvation parameters recovered by the extended solvation model suggesting destabilization of the protein

Thermodynamic Study of Comfarol Binding to Urease

Isothermal Titration Calorimetry, ITC, was used to study of Jack Bean urease, JBU, binding with comfarol in phosphate buffer at pH 7.4. Data analyzing of comfarol interaction with JBU was performed by the extended solvation model and the positive cooperativity of comfarol with JBU indicates that comfarol causes stabilization of the JBU structure. DOI: http://dx.doi.org/10.17807/orbital.v11i3.1369</p