Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cyclodextrin-induced host-guest effects of classically prepared poly(NIPAM) bearing azo-dye end groups.

ABSTRACT: A thermo-, pH- and cyclodextrin- (CD) responsive poly(N-isopropylacrylamide) (PNIPAM), with a N,N-dimethylaminoazobenzene end group was synthesized. Using 3-mercaptopropionic acid as a chain transfer agent, PNIPAM with a well-defined COOH end group was obtained. The acid end group was transferred to the corresponding acid chloride and then functionalized with N,N-dimethyl[4-(4'-aminophenylazo)phenyl]amine. This dye-end-group-labeled polymer showed acidochromic effects, depending on the pH and the presence of randomly methylated ?-cyclodextrin (RAMEB-CD). Also higher cloud-point values for the lower critical solution temperature (LCST) in the presence of RAMEB-CD were observed. Additionally, this azo-dye-end-group-labeled polymer was complexed with hyperbranched polyglycerol (HPG) decorated with ?-CD to generate hedgehog-like superstructures.

SUBMITTER: Maatz G

PROVIDER: S-EPMC3511033 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Cyclodextrin-induced host-guest effects of classically prepared poly(NIPAM) bearing azo-dye end groups.

Maatz Gero G Maciollek Arkadius A Ritter Helmut H

Beilstein journal of organic chemistry 20121114

A thermo-, pH- and cyclodextrin- (CD) responsive poly(N-isopropylacrylamide) (PNIPAM), with a N,N-dimethylaminoazobenzene end group was synthesized. Using 3-mercaptopropionic acid as a chain transfer agent, PNIPAM with a well-defined COOH end group was obtained. The acid end group was transferred to the corresponding acid chloride and then functionalized with N,N-dimethyl[4-(4'-aminophenylazo)phenyl]amine. This dye-end-group-labeled polymer showed acidochromic effects, depending on the pH and th ...[more]

PMID: 23209533

Similar Datasets

Hyperbranched polyethylenimine bearing cyclodextrin moieties showing temperature and pH controlled dye release.

Project description:The release of anthraquinone dyes from ?-cyclodextrin modified, hyperbranched polyethylenimine (PEI-CD) was investigated. 5,8-Dichloro-1,4-dihydroxyanthraquinone (AQ-OH) was enclosed simply by ionic attraction between the phenolate groups of AQ-OH and the protonated amino groups of polyethylenimine (PEI). Additionally, the adamantyl moieties of 1,4-bis-N-adamantylaminoanthraquinone (AQ-Ada) were encapsulated by the cavity of CD modified PEI. Due to these different types of interaction, the dyes can be controllably released from the CD-cavity (AQ-Ada) by temperature variation or from salt encapsulation by pH variation (AQ-OH), as monitored by UV-vis spectroscopy.

| S-EPMC3167151 | biostudies-literature

Effects of azo dye on simultaneous biological removal of azo dye and nutrients in wastewater.

Project description:The potential disrupting effects of Azo dye on wastewater nutrients removal deserved more analysis. In this study, 15 days exposure experiments were conducted with alizarin yellow R (AYR) as a model dye to determine whether the dye caused adverse effects on biological removal of both the dye and nutrients in acclimated anaerobic-aerobic-anoxic sequencing batch reactors. The results showed that the AYR removal efficiency was, respectively, 85.7% and 66.8% at AYR concentrations of 50 and 200 mg l-1, while higher AYR inlet (400 mg l-1) might inactivate sludge. Lower removal of AYR at 200 mg l-1 of AYR was due to the insufficient support of electron donors in the anaerobic process. However, the decolorized by-products p-phenylenediamine and 5-aminosalicylic were completely decomposed in the following aerobic stage at both 50 and 200 mg l-1 of AYR concentrations. Compared with the absence of AYR, the presence of 200 mg l-1 of AYR decreased the total nitrogen removal efficiency from 82.4 to 41.1%, and chemical oxygen demand (COD) removal efficiency initially decreased to 68.1% and then returned to around 83.4% in the long-term exposure time. It was also found that the inhibition of AYR, nitrogen and COD removal induced by a higher concentration of AYR was due to the increased intracellular reactive oxygen species production, which caused the rise of oxidation-reduction potential value and decreased ammonia monooxygenase and nitrite oxidoreductase activities.

| S-EPMC6124032 | biostudies-literature

Recent advances in azo dye degrading enzyme research.

Project description:Azo dyes, which are characterized by one or more azo bonds, are a predominant class of colorants used in tattooing, cosmetics, foods, and consumer products. These dyes are mainly metabolized by bacteria to colorless aromatic amines, some of which are carcinogenic, by azoreductases that catalyze a NAD(P)H-dependent reduction. The resulting amines are further degraded aerobically by bacteria. Some bacteria have the ability to degrade azo dyes both aerobically and anaerobically. Plant-degrading white rot fungi can break down azo dyes by utilizing a number of oxidases and peroxidases as well. In yeast, a ferric reductase system participates in the extracellular reduction of azo dyes. Recently, two types of azoreductases have been discovered in bacteria. The first class of azoreductases is monomeric flavin-free enzymes containing a putative NAD(P)H binding motif at their N-termini; the second class is polymeric flavin dependent enzymes which are studied more extensively. Azoreductases from bacteria represent novel families of enzymes with little similarity to other reductases. Dissociation and reconstitution of the flavin dependent azoreductases demonstrate that the non-covalent bound flavin prosthetic group is required for the enzymatic functions. In this review, structures and carcinogenicity of azo colorants, protein structure, enzymatic function, and substrate specificity, as well as application of the azo dyes and azoreductases will be discussed.

| S-EPMC5863238 | biostudies-literature

The cobalt(II) salt of the azo dye Orange G.

Project description:Crystallizing the cobalt(II) salt of the azo dye Orange G from water was found to give the solvent-separated ion-pair species hexa-aqua-cobalt(II) 7-oxo-8-(2-phenyl-hydrazin-1-ylidene)-7,8-dihydro-naphthalene-1,3-disulfonate tetra-hydrate, [Co(H(2)O)(6)](C(16)H(10)N(2)O(7)S(2))·4H(2)O. The asymmetric unit of the cobalt(II) salt contains three independent octa-hedral [Co(OH(2))(6)](2+) cations, three azo anions, all with similar configurations, and 12 uncoordinated water mol-ecules. The structure is closely related to that of one of the known magnesium analogues. Both structures have Z' = 3, feature nearly planar azo anions [maximum displacement of azo-N atoms from the plane of the phenyl ring = 0.058?(7)?Å] in their hydrazone tautomeric form, form layer structures with hydro-philic and hydro-phobic layers alternating along the b-axis direction, and are stabilized by an extensive network of hydrogen bonds..

| S-EPMC2983163 | biostudies-literature

Azo dye biodecolorization enhanced by Echinodontium taxodii cultured with lignin.

Project description:Lignocellulose facilitates the fungal oxidization of recalcitrant organic pollutants through the extracellular ligninolytic enzymes induced by lignin in wood or other plant tissues. However, available information on this phenomenon is insufficient. Free radical chain reactions during lignin metabolism are important in xenobiotic removal. Thus, the effect of lignin on azo dye decolorization in vivo by Echinodontium taxodii was evaluated. In the presence of lignin, optimum decolorization percentages for Remazol Brilliant Violet 5R, Direct Red 5B, Direct Black 38, and Direct Black 22 were 91.75% (control, 65.96%), 76.89% (control, 43.78%), 43.44% (control, 17.02%), and 44.75% (control, 12.16%), respectively, in the submerged cultures. Laccase was the most important enzyme during biodecolorization. Aside from the stimulating of laccase activity, lignin might be degraded by E. taxodii, and then these degraded low-molecular-weight metabolites could act as redox mediators promoting decolorization of azo dyes. The relationship between laccase and lignin degradation was investigated through decolorization tests in vitro with purified enzyme and dozens of aromatics, which can be derivatives of lignin and can function as laccase mediators or inducers. Dyes were decolorized at triple or even higher rates in certain laccase-aromatic systems at chemical concentrations as low as 10 µM.

| S-EPMC4186836 | biostudies-literature

Platinum(IV)-Ferrocene Conjugates and Their Cyclodextrin Host-Guest Complexes.

Project description:Reported here are new platinum(IV) (Pt(IV)) complexes bearing ferrocene (Fc) moieties. These systems differ from one another only by the nature of the functional group (ester vs amide) connecting the linker to the Fc subunits. This minor structural variation (one atom difference) leads to major differences in solubility, stability, and antiproliferative activity against lung (A549) cancer cells. The host-guest chemistry of these complexes was investigated in an aqueous medium in the presence of β-cyclodextrins (β-CD), either free or in the form of a covalently linked Fc-Pt-β-CD hybrid. An inclusion complex between Fc and β-CD is formed in aqueous media, presumably as a result of hydrophobic interactions involving the Fc and the inner β-CD cavity. Consequently, it proved possible to use a β-CD-based strategy to purify the Pt-Fc conjugates in this study under aqueous conditions (by means of C18 silica gel columns). The use of a β-CD adjuvant also allowed dimethyl sulfoxide (DMSO) to be avoided as an organic cosolvent in cell studies. The amide version reported here (2) proved to be more soluble, more stable, and more active than the ester analogue (11) in A549 cells. The use of a β-CD functionalized with a fluorescent probe allowed intracellular Pt-Fc localization to be visualized by confocal fluorescence microscopy.

| S-EPMC6953482 | biostudies-literature

Experimental characterization of the association of β-cyclodextrin and eight novel cyclodextrin derivatives with two guest compounds.

Project description:We investigate the binding of native β-cyclodextrin (β-CD) and eight novel β-CD derivatives with two different guest compounds, using isothermal calorimetry and 2D NOESY NMR. In all cases, the stoichiometry is 1:1 and binding is exothermic. Overall, modifications at the 3' position of β-CD, which is at the secondary face, weaken binding by several kJ/mol relative to native β-CD, while modifications at the 6' position (primary face) maintain or somewhat reduce the binding affinity. The variations in binding enthalpy are larger than the variations in binding free energy, so entropy-enthalpy compensation is observed. Characterization of the bound conformations with NOESY NMR shows that the polar groups of the guests may be situated at either face, depending on the host molecule, and, in some cases, both orientations are populated. The present results were used in the SAMPL7 blinded prediction challenge whose results are detailed in the same special issue of JCAMD.

| S-EPMC7867601 | biostudies-literature

Genome sequence of Enterococcus sp. strain C1, an azo dye decolorizer.

Project description:Enterococcus sp. strain C1 is a facultative anaerobe which was coisolated with Citrobacter sp. strain A1 from a sewage oxidation pond. Strain C1 could degrade azo dyes very efficiently via azo reduction and desulfonation in a microaerophilic environment. Here the draft genome sequence of Enterococcus sp. C1 is reported.

| S-EPMC3458668 | biostudies-literature

Probing horseradish peroxidase catalyzed degradation of azo dye from tannery wastewater.

Project description:Biocatalysis based effluent treatment has outclassed the presently favored physico-chemical treatments due to nil sludge production and monetary savings. Azo dyes are commonly employed in the leather industry and pose a great threat to the environment. Here, we show the degradation of C. I. Acid blue 113 using horseradish peroxidase (HRP) assisted with H2O2 as a co-substrate. It was observed that 0.08 U HRP can degrade 3 mL of 30 mg/L dye up to 80% within 45 min with the assistance of 14 ?L of H2O2 at pH 6.6 and 30°C. The feasibility of using the immobilized HRP for dye degradation was also examined and the results show up to 76% dye degradation under similar conditions to that of free HRP with the exception of longer contact time of 240 min. Recycling studies reveal that the immobilized HRP can be recycled up to 3 times for dye degradation. Kinetics drawn for the free HRP catalyzed reaction marked a lower K m and higher V max values, which denotes a proper and faster affinity of the enzyme towards the dye, when compared to the immobilized HRP. The applicability of HRP for treating the actual tannery dye-house wastewater was also demonstrated.

| S-EPMC3736071 | biostudies-literature

Dye-sensitized solar cells based on a push-pull zinc phthalocyanine bearing diphenylamine donor groups: computational predictions face experimental reality.

Project description:Computational studies have suggested that the integration of secondary amine as donor groups in the structure of unsymmetrical zinc phthalocyanine (ZnPc) should have positive effects on photovoltaic performance, once the molecule is integrated as light harvester in dye sensitized solar cells (DSSCs). Aiming at obtaining experimental confirmation, we synthesized a peripherally substituted push-pull ZnPc bearing three electron donating diphenylamine substituents and a carboxylic acid anchoring group and integrated it as sensitizer in TiO2-based DSSCs. Detailed functional characterization of solar energy converting devices resulted in ruling out the original hypothesis. The causes of this discrepancy have been highlighted, leading to a better understanding of the conditions for an effective design of push-pull diarylamino substituted ZnPcs for DSSCs.

| S-EPMC5688058 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data