191 research outputs found
Interaction between Aniline Derivatives and Single-Walled Carbon Nanotubes Investigated by Fluorescence and Quantum-Chemical Methods
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Interactions of zearalanone, α-zearalanol, β-zearalanol, zearalenone-14-sulfate, and zearalenone-14-glucoside with serum albumin
De vluchtige olie van mentha piperita L. gedurende de ontwikkeling van de plant
After a short description of the plant, the culture and the chemical composition of peppermint oil, a method is suggested for the determtnation of the total number of glandular hairs on the leaf. A new colorimetric determination of menthone and menthol, usins 2,4 - dinitr ophenylhy & azine is elaborated. ... Zie: Summar
Fluorescence spectroscopic evaluation of the interactions of quercetin, isorhamnetin, and quercetin-3'-sulfate with different albumins
Quercetin is one of the most commonly occurring flavonoids in nature. Although, quercetin and its metabolites express negligible fluorescence, the albumin-bound form of quercetin has a strong fluorescence property. Considering the structural variance of different albumins, we hypothesized that the fluorescence of albumin complexes of quercetin and its metabolites may vary significantly. Therefore, in this study the fluorescence enhancement of quercetin and some of its major metabolites in the presence of bovine (BSA), human (HSA), porcine (PSA), and rat serum albumins (RSA) were investigated by steady-state fluorescence spectroscopy in PBS buffer (pH 7.4). Among the tested quercetin metabolites, significant fluorescence signal was shown by albumin complexes of quercetin, isorhamnetin, and quercetin-3’-sulfate, while other metabolites (tamarixetin, quercetin-3-glucuronide, and isorhamnetin-3-glucuronide) expressed negligible fluorescence. BSA was the most potent enhancer of quercetin-3’-sulfate but it showed poor effects regarding other flavonoids. The strongest enhancement of isorhamnetin was caused by HSA, while it was less effective enhancer of quercetin and quercetin-3’-sulfate. PSA showed a strong fluorescence enhancement of quercetin and quercetin-3’-sulfate but it was poorly effective regarding isorhamnetin. RSA was the most potent enhancer of quercetin but it caused only a weak enhancement of isorhamnetin and quercetin-3’-sulfate. Large changes of the pH (such as pH 5.0 and pH 10.0) almost completely abolished the fluorescence signals of the complexes. Nevertheless, slight decrease (pH 7.0) reduced and slight increase (pH 7.8) generally enhanced the fluorescence of flavonoid-albumin complexes (only exceptions were quercetin-PSA and quercetin-RSA). Complex formations were also investigated by fluorescence quenching studies. Based on our results, the formations of quercetin-BSA, quercetin-HSA, isorhamnetin-BSA, isorhamnetin-HSA, isorhamnetin-PSA, and quercetin-3’-sulfate – HSA complexes followed 1:1 stoichiometry, while the presence of a secondary binding site of flavonoids was assumed regarding other tested albumin complexes. Our study highlights that albumins can induce significantly different fluorescence enhancement of flavonoids, and even the stoichiometry of flavonoid-albumin complexes may differ
Interaction of zearalenone-14-sulfatewith cyclodextrins and the removal of the modified mycotoxin from aqueous solution by beta-cyclodextrin bead polymer
Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes
Probing the interactions of ochratoxin B, ochratoxin C, patulin, deoxynivalenol, and T-2 toxin with human serum albumin
Ochratoxins, patulin, deoxynivalenol, and T-2 toxin are mycotoxins, and common contaminants in food and drinks. Human serum albumin (HSA) forms complexes with certain mycotoxins. Since HSA can affect the toxicokinetics of bound ligand molecules, the potential interactions of ochratoxin B (OTB), ochratoxin C (OTC), patulin, deoxynivalenol, and T-2 toxin with HSA were examined, employing spectroscopic (fluorescence, UV, and circular dichroism) and ultrafiltration techniques. Furthermore, the influence of albumin on the cytotoxicity of these xenobiotics was also evaluated in cell experiments. Fluorescence studies showed the formation of highly stable OTB–HSA and OTC–HSA complexes. Furthermore, fluorescence quenching and circular dichroism measurements suggest weak or no interaction of patulin, deoxynivalenol, and T-2 toxin with HSA. In ultrafiltration studies, OTB and OTC strongly displaced the Sudlow’s site I ligand warfarin, while other mycotoxins tested did not affect either the albumin binding of warfarin or naproxen. The presence of HSA significantly decreased or even abolished the OTB- and OTC-induced cytotoxicity in cell experiments; however, the toxic impacts of patulin, deoxynivalenol, and T-2 toxin were not affected by HSA. In summary, the complex formation of OTB and OTC with albumin is relevant, whereas the interactions of patulin, deoxynivalenol, and T-2 toxin with HSA may have low toxicological importance
Interaction of α- and β-zearalenols with β-cyclodextrins
Zearalenone (ZEN) is a mycotoxin produced by Fusarium fungi. ZEN primarily contaminates different cereals, and exerts a strong xenoestrogenic effect in animals and humans. ZEN is a fluorescent mycotoxin, although molecular interactions and microenvironmental changes significantly modify its spectral properties. During biotransformation, ZEN is converted into α-zearalenol (α-ZOL) and β-zearalenol (β-ZOL), the toxic metabolites of ZEN, which mimick the effect of estrogen. Cyclodextrins (CDs) are host molecules, and have been studied extensively; they can form stable complexes with several mycotoxins, including ZEN. However, information is limited regarding the interactions of CDs with ZOLs. Therefore, we studied the interactions of α- and β-ZOLs with native and six chemically modified β-CDs by fluorescence spectroscopy. Fluorescence enhancement during complex formation, as well as binding constants, were determined. To understand ZOL-CD interactions better, molecular modeling studies were also carried out. Both mycotoxin derivatives formed the most stable complexes with methylated and sulfobutylated CD-derivatives; however, the CD complexes of α-ZOL were significantly stronger than those of β-ZOL. The data presented here indicate which of the chemically modified β-CDs appear more suitable as fluorescence enhancers or as potential mycotoxin binders
Interactions of Mycotoxin Alternariol with Cyclodextrins and its Removal from Aqueous Solution by Beta-Cyclodextrin Bead Polymer
Alternariol is an Alternaria mycotoxin that appears in fruits, tomatoes, oilseeds, and corresponding products. Chronic exposure to it can induce carcinogenic and xenoestrogenic effects. Cyclodextrins (CDs) are ring-shaped molecules built up by glucose units, which form host–guest type complexes with some mycotoxins. Furthermore, insoluble CD polymers seem suitable for the extraction/removal of mycotoxins from aqueous solutions. In this study, the interactions of alternariol with β- and γ-CDs were tested by employing fluorescence spectroscopic and modeling studies. Moreover, the removal of alternariol from aqueous solutions by insoluble β-CD bead polymer (BBP) was examined. Our major observations/conclusions are the following: (1) CDs strongly increased the fluorescence of alternariol, the strongest enhancement was induced by the native γ-CD at pH 7.4. (2) Alternariol formed the most stable complexes with the native γ-CD (logK = 3.2) and the quaternary ammonium derivatives (logK = 3.4–3.6) at acidic/physiological pH and at pH 10.0, respectively. (3) BBP effectively removed alternariol from aqueous solution. (4) The alternariol-binding ability of β-CD polymers was significantly higher than was expected based on their β-CD content. (5) CD technology seems a promising tool to improve the fluorescence detection of alternariol and/or to develop new mycotoxin binders to decrease alternariol exposure
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