Presence Of Congo Red Research Articles

Novel synthesis of advanced Cu capped Cu2O nanoparticles and their photo-catalytic activity for mineralization of aqueous dye molecules

In current study, Cu capped Cu2O nanoparticles (Cu-Cu2O) was synthesized using trioctylamine which is playing a dual role as a hydrolyzing agent as well as capping agent. Temperature and time dependent studies were also performed to monitor different phase formation. As synthesized material was characterized by X-ray diffraction (XRD) for phase determination, crystalline size and morphological investigation. Transmission electron microscopy (TEM) images revels the morphology of the nanoparticles was cubic which leads to spherical at higher temperature. Photocatalytic mineralization studies were carried out in the presence of Congo Red (CR) dye, organic molecules decontamination from aquatic environment with 98.7% mineralization.

Decolorization of Congo Red by Phanerochaete chrysosporium: the role of biosorption and biodegradation

ABSTRACTThe degradation of Congo Red by means of Phanerochaete chrysosporium BKM-F-1767 is reported in this work. Solid and liquid cultures have been prepared to evaluate in vivo biodegradation as well as the role of biosorption phenomena on mycelium. Moreover, in vitro tests have been performed to define the influence of MnP on dye decolorization. P. chrysosporium, cultivated on Malt Extract Agar in the presence of Congo Red 0.005% (w/v), has shown good growth and the ability to decolorize the dye in the 25–39°C temperature range. It has also been cultivated in a low NMM liquid medium with the aforementioned dye concentration in immobilized stationary cultures inducted for Lignin Peroxidase (LiP) and Manganese Peroxidase (MnP) production. Congo Red was absorbed on the biomass and then decolorized (93% and 85% for the LiP and MnP cultures, respectively). The cultures with added Congo Red have shown a higher MnP synthesis rate than a control without the dye. The enzymatic degradation of Congo Red has also been investigated by means of the extracellular fluid for different MnP activities (0–300 IU/l); the decolorization percentage has been found to be clearly related to the enzyme concentration up to a value of about 200 IU/l.

Electrochemical Synthesis of Polypyrrole in the Presence of Congo Red; Application to Selective Voltammetric Determination of Dopamine in the Presence of Ascorbic Acid

AbstractThe electrosynthesis of polypyrrole (PPy) film has been achieved on glassy carbon electrode (GCE) in aqueous medium of Congo red (CR) by means of cyclic voltammetry (CV). The modified electrode exhibits high electrocatalytic activity toward dopamine (DA) oxidation, with drastic enhancement of the reversibility and peak currents. This modified electrode, due to electrostatic interactions, is capable to mask the response of ascorbic acid (AA) completely and provide an effective method for the detection of minor amounts of dopamine in the presence of high concentrations of AA. The electrochemical response of the film modified electrode is strongly dependent to the switching potential applied in the CV procedure of the electro‐polymerization. The results show that by increasing the switching potential more than 0.75 V, the peak of AA is gradually disappeared. This peak in potential of 0.85 V is reached to capacitive background current. With respect to the destruction of the conjugated structure of ppy and lowering the conductivity of the film at the surface of modified electrode, higher switching potentials cannot be suitable for electropolymerization procedure. The effects of various experimental parameters such as, number of polymerization cycles, switching potential, pH and potential sweep rate on the voltammetric response of dopamine were also investigated. The modified electrode shows a linear response to DA in the range of 0.5 to 100 μM with a detection limit of 0.1 μM. The prepared modified electrode does not show any considerable response toward sulfhydryl compounds, such as, cysteine, penicillamine and glutathione, revealing a good selectivity for voltammetric response to DA. The effective electrocatalytic property, ability for masking the voltammetric responses of the other biological reducing agents together with high reproducibility and stability make the modified electrode suitable for selective and sensitive voltammetric detection of sub‐micromolar amounts of DA in clinical and pharmaceutical preparations.

Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes

A key factor in the development of Type II diabetes is the loss of insulin producing pancreatic β-cells. The amyloidogenic human Islet Amyloid Polypeptide (hIAPP also known as human amylin) is believed to play a crucial role in this biological process. Previous studies have shown that hIAPP forms small aggregates that kill β-cells by disrupting the cellular membrane. In this study, we report membrane fragmentation by hIAPP using solid-state NMR experiments on nanotube arrays of anodic aluminum oxide containing aligned phospholipid membranes. In a narrow concentration range of hIAPP, an isotropic 31P chemical shift signal indicative of the peptide-induced membrane fragmentation was detected. Solid-state NMR results suggest that membrane fragmentation is related to peptide aggregation as the presence of Congo Red, an inhibitor of amyloid formation, prevented membrane fragmentation and the non-amyloidogenic rat-IAPP did not cause membrane fragmentation. The disappearance of membrane fragmentation at higher concentrations of hIAPP suggests an alternate kinetic pathway to fibril formation in which membrane fragmentation is inhibited.

Effect of congo red on the motility of the bacterium Azospirillum brasilense

In semiliquid laboratory media, the bacterium Azospirillum brasilense migrates with the formation of swarming rings. It is demonstrated that adsorption of the sulfonated azodye Congo Red confers on A. brasilense the ability to consistently spread in a semiliquid agar and form microcolonies. Spontaneous variants of A. brasilense with rapid swarming are described, as well as variants that swarm in the presence of Congo Red. It is assumed that at least two types of compounds are formed, which are (a) necessary for swarming and/or spreading with the formation of microcolonies and (b) capable of interacting with Congo Red.

Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops.

Human apolipoprotein C-II (apoC-II) self-associates in solution to form aggregates with the characteristics of amyloid including red-green birefringence in the presence of Congo Red under cross-polarized light, increased fluorescence in the presence of thioflavin T, and a fibrous structure when examined by electron microscopy. ApoC-II was expressed and purified from Escherichia coli and rapidly exchanged from 5 M guanidine hydrochloride into 100 mM sodium phosphate, pH 7.4, to a final concentration of 0.3 mg/mL. This apoC-II was initially soluble, eluting as low molecular weight species in gel filtration experiments using Sephadex G-50. Circular dichroism (CD) spectroscopy indicated predominantly unordered structure. Upon incubation for 24 h, apoC-II self-associated into high molecular weight aggregates as indicated by elution in the void volume of a Sephadex G-50 column, by rapid sedimentation in an analytical ultracentrifuge, and by increased light scattering. CD spectroscopy indicated an increase in beta-sheet content, while fluorescence emission spectroscopy of the single tryptophan revealed a blue shift and an increase in maximum intensity, suggesting repositioning of the tryptophan into a less polar environment. Electron microscopy of apoC-II aggregates revealed a novel looped-ribbon morphology (width 12 nm) and several isolated closed loops. Like all of the conserved plasma apolipoproteins, apoC-II contains amphipathic helical regions that account for the increase in alpha-helix content on lipid binding. The increase in beta-structure accompanying apoC-II fibril formation points to an alternative folding pathway and an in vitro system to explore the general tendency of apolipoproteins to form amyloid in vivo.

PAPER ELECTROPHORESIS OF HEAT-TREATED SERUM ALBUMIN IN THE PRESENCE OF CONGO RED.

IT is known that if the specific spatial arrangement of the peptide chains of some proteins, such as egg albumin and serum albumin, is altered by heat, they coagulate and lose many of their specific properties. This phenomenon of denaturation is generally irreversible.