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Novel synthetic routes to furan fatty acids and their analoguesWang, Yamin January 2016 (has links)
Furan and its derivatives are commonly found in numerous compounds such as natural products, polymers and medicines. The furan ring system is not only the core component to many natural products, but also serves as a key synthetic intermediate to access other more complex molecules. Among furan derivatives, furan fatty acids (F-acids) are an important class of natural products which are widely distributed in nature, and occupy a unique place in the field of medicinal chemistry because of their potent biological and pharmacological activity. This thesis examines the development of novel approaches towards highly substituted furans, with the ultimate goal of applying novel and high efficiency methods to the synthesis of F-acids and their derivatives. The first total synthesis of a natural product, an F-acids metabolite originally isolated from shark (Lamna ditropis) bile, was accomplished by the utilisation of an iodocyclisation of the corresponding 3-alkyne-1,2-diol to construct the furan nucleus; the synthetic route will be discussed in this thesis. Through the study of palladium-catalysis of a formal cyclisation to construct the furan ring system, a general route to access different F-acids has been developed. Splitting the F-acids into relatively simple fragments allows for easy preparation and modification of two fragments to produce a range of F-acids. The synthetic route was then applied to the formal synthesis of a natural product, F-acid F6. After optimisation of the synthetic route, total synthesis of F-acids F4, F6 and their analogues was accomplished.
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The preparation and modification of polyvinylfuran, copolymers of vinylfuran and styrene, and polyacenaphthyleneDillingham, Keith Alfred January 1994 (has links)
No description available.
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Alkylation of furan with 2-phenylthioallyl chlorideGains, Lawrence Howard, 1948- January 1977 (has links)
No description available.
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Synthesis of substituted furans and thiophenesMorrison, B. J. January 1984 (has links)
No description available.
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Untersuchungen zum Metabolismus von Furan in Ratte und Maus, sowie zur Reaktivität und Gentoxizität von cis-2-Buten-1,4-dial in vitro und in ZellkulturKellert, Marco. Unknown Date (has links) (PDF)
Würzburg, Universiẗat, Diss., 2008.
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Design and synthesis of novel donor-acceptor-donor xanthene-based dyes from heteronuclear ring systems for chemical, electrochemical, and biological sensory materialsRajapaksha, Ishanka Nirmani 09 December 2022 (has links) (PDF)
Conventional xanthene dyes (eg: fluorescein and rhodamine) have their absorptions and emissions in the visible region, which limits their use in cellular imaging. Absorptions and emissions at longer wavelengths allow for low background cellular autofluorescence, deep tissue penetration, and minimum cell damage. Chapter I discusses the background of fluorescent dyes and the importance of near-infrared (NIR) emissive dyes for biological applications. Chapter II is based on the design and synthesis of new xanthene-based NIR I dyes using simple and short synthetic routes. This study used pyrrole and indole as donor molecules and combined them to the xanthene core by the Suzuki cross-coupling reaction to prepare the new dyes. After the treatment with trifluoroacetic acid, these new dyes transformed from their non-fluorescent to fluorescent forms and exhibited excellent red shifts in their maximum absorption and emission wavelengths. The novel pyrrole-based xanthene dye was used to investigate the efficacy of the dye as a probe for fluoride ions. We were able to modify this dye with a silyl ester receptor and develop a probe as a colorimetric turn-off fluoride ion sensor. In chapter III, we describe the synthesis of different NIR emissive xanthene dyes using the donor-acceptor-donor concept. New xanthene-based dyes were designed with five-membered heterocycles and fused heteronuclear molecules. Additionally, xanthene-based dyes containing an alkyne spacer were synthesized using the D-pi-A model to extend the pi-conjugation through the alkyne spacer. All of the dyes exhibited absorption and emission maxima in the visible to NIR I region, between 500-850 nm.
In chapter IV, we discussed the synthesis of xanthene-based electrochromic materials. These compounds used xanthene as the chromophore and ferrocene as the electrophore units. Novel rhodamine-based symmetric and unsymmetric dyes were synthesized by attaching the ferrocene unit through the lactam ring. The compounds were then investigated as an electrochromic probe using UV-Vis, cyclic voltammetry, and spectroelectrochemical analysis.
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Synthetic studies towards the squalestatinsMontagnon, T. January 2000 (has links)
No description available.
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Identification of target proteins of furan reactive metabolites in rat liver / Identifizierung von Zielproteinen reaktiver Furan-Metabolite in RattenleberMoro, Sabrina January 2011 (has links) (PDF)
Furan was recently found to be present in a variety of food items that undergo heat treatment. It is known to act as a potent hepatotoxin and liver carcinogen in rodents. In a 2-year bioassay, chronic furan administration to rats was shown to cause hepatocellular adenomas and carcinomas and very high incidences of cholangiocarcinomas even at the lowest furan dose tested (2.0 mg/kg bw). However, the mechanisms of furan-induced tumor formation are poorly understood. Furan is metabolized by cytochrome P450 (CYP) enzymes, predominantly CYP2E1, to its major metabolite cis-2-butene-1,4-dial (BDA). BDA is thought to be the key mediator of furan toxicity and carcinogenicity and was shown to react with cellular nucleophiles such as nucleosides and amino acid residues in vitro. It is well known that covalent protein binding may lead to cytotoxicity, but the cellular mechanisms involved remain to be elucidated. Since covalent binding of reactive intermediates to a target protein may result in loss of protein function and subsequent damage to the cell, the aim of this study was to identify furan target proteins to establish their role in the pathogenesis of furan-associated liver toxicity and carcinogenicity. In order to identify target proteins of furan reactive metabolites, male F344/N rats were administered [3,4-14C]-furan. Liquid scintillation counting of protein extracts revealed a dose-dependent increase of radioactivity covalently bound to liver proteins. After separation of the liver protein extracts by two-dimensional gel electrophoresis and subsequent detection of radioactive spots by fluorography, target proteins of reactive furan intermediates were identified by mass spectrometry and database search via Mascot. A total of 61 putative target proteins were consistently found to be adducted in 3 furan-treated rats. The identified proteins represent - among others - enzymes, transport proteins, structural proteins and chaperones. Pathway mapping tools revealed that target proteins are predominantly located in the cytosol and mitochondria and participate in glucose metabolism, mitochondrial β-oxidation of fatty acids, and amino acid degradation. These findings together with the fact that ATP synthase β subunit was also identified as a putative target protein strongly suggest that binding of furan reactive metabolites to proteins may result in mitochondrial injury, impaired cellular energy production, and altered redox state, which may contribute to cell death. Moreover, several proteins involved in the regulation of redox homeostasis represent putative furan target proteins. Loss of function of these proteins by covalent binding of furan reactive metabolites may impair cellular defense mechanisms against oxidative stress, which may also result in cell death. Besides the potential malfunction of whole pathways due to loss of functions of several participating proteins, loss of function of individual proteins which are involved in various cellular processes such as transport processes across the mitochondrial membranes, cell signaling, DNA methylation, blood coagulation, and bile acid transport may also contribute to furan-induced cytotoxicity and carcinogenicity. Covalent binding of reactive metabolites to cellular proteins may result in accumulation of high amounts of unfolded or damaged proteins in the endoplasmic reticulum (ER). In response to this ER stress, the cell can activate the unfolded protein response (UPR) to repair or degrade damaged proteins. To address whether binding of furan reactive metabolites to cellular proteins triggers activation of the UPR, semiquantitative PCR and TaqMan® real-time PCR were performed. In the case of UPR activation, semiquantitative PCR should show enhanced splicing of X-box binding protein-1 (XBP1) mRNA (transcription factor and key regulator of the UPR) and TaqMan® real-time PCR should determine an increased expression of UPR target genes. However, our data showed no evidence for activation of the UPR in the livers of rats treated either with a single hepatotoxic dose or with a known carcinogenic dose for 4 weeks. This suggests either that furan administration does not induce ER stress through accumulation of damaged proteins or that activation of the UPR is disrupted. Consistent with the latter, glucose-regulated protein 78 (GRP78), identified as a target protein in our study, represents an important mediator involved in activation of the UPR whose inhibition was shown to impair induction of the UPR. Thus, adduct formation and inactivation of GRP78 by furan metabolites may disturb activation of the UPR. In addition to impaired activation of UPR, protein repair and degradation functions may be altered, because several proteins involved in these processes also represent target proteins of furan and thus may show impaired functionality. Taken together... / Im Rahmen von Untersuchungen der U.S. Food and Drug Administration (FDA) wurde im Jahr 2004 bekannt, dass Furan in verschiedensten hitzebehandelten Lebensmitteln vorkommt. Durch Tierstudien des National Toxicology Programs (NTP) aus den 90er Jahren wusste man bereits, dass Furan hepatotoxische und leberkanzerogene Wirkungen in Nagern verursacht. In diesen Studien wurden nach chronischer Verabreichung von Furan an Ratten über einen Zeitraum von 2 Jahren bereits bei der niedrigsten getesteten Dosis von 2 mg/kg Körpergewicht hepatozelluläre Adenome und Karzinome sowie sehr hohe Inzidenzen von Cholangiokarzinomen beobachtet. Die Mechanismen, die der Tumorentstehung durch Furan zugrunde liegen, sind jedoch bis heute nicht ausreichend untersucht. Furan wird durch Enzyme der Cytochrom P450 (CYP) Familie, vor allem durch CYP2E1, zu seinem Hauptmetaboliten cis-2-Buten-1,4-dial (BDA) verstoffwechselt. Der reaktive Furan-Metabolit BDA kann in vitro mit zellulären Nukleophilen wie Nukleosiden und Aminosäureresten reagieren. Verschiedene Untersuchungen weisen darauf hin, dass die toxischen und kanzerogenen Effekte von Furan hauptsächlich durch BDA vermittelt werden. Es ist seit langem bekannt, dass kovalente Bindung an Proteine zu Zytotoxizität führen kann. Der zugrunde liegende Mechanismus ist bislang noch ungeklärt. Es wird jedoch vermutet, dass die kovalente Bindung von reaktiven Metaboliten an Proteine zu deren Funktionsverlust führt, was wiederum fatale Konsequenzen für die Zellen haben kann. Eine Identifizierung der Zielproteine von Furan, d.h. jener Proteine an denen eine Adduktbildung durch reaktive Metabolite von Furan erfolgt, könnte daher Aufschluss über deren mögliche Rolle in der Pathogenese der durch Furan induzierten Lebertoxizität und -kanzerogenität geben. Um die Zielproteine reaktiver Furan-Metabolite zu identifizieren, wurde [3,4-14C]-Furan an männliche F344/N Ratten verabreicht. Durch Flüssigkeitsszintillationszählung der Proteinextrakte wurde ein dosisabhängiger Anstieg der kovalent an Leberproteine gebundenen Radioaktivität ermittelt. Nach der Auftrennung der Leberproteinextrakte durch zweidimensionale Gelelektrophorese und der Detektion der radioaktiven Spots durch Fluorographie wurden die Zielproteine reaktiver Furan-Metabolite durch Massenspektrometrie und Datenbanksuche (Mascot-Datenbank) identifiziert. In 3 Ratten, die mit Furan behandelt worden waren, wurden übereinstimmend 61 mögliche Zielproteine von Furan identifiziert. Unter diesen Zielproteinen waren unter anderem Enzyme, Transportproteine, Strukturproteine und Chaperones vertreten. Die Zuordnung der identifizierten Proteine zu zellulären Signal- und Stoffwechselwegen mittels spezieller Software zeigte, dass die Zielproteine hauptsächlich aus dem Zytosol und den Mitochondrien stammen und an Glucosemetabolismus, mitochondrieller β-Oxidation von Fettsäuren und dem Abbau von Aminosäuren beteiligt sind. Außerdem wurde auch die β-Untereinheit der ATP-Synthase als mögliches Zielprotein identifiziert. Diese Ergebnisse weisen stark darauf hin, dass die Bindung reaktiver Furan-Metabolite an Proteine zur Schädigung der Mitochondrien, Beeinträchtigung der zellulären Energieproduktion und verändertem Redox-Status führen und damit zum Zelltod beitragen könnte. Weiterhin befanden sich unter den möglichen Zielproteinen auch Proteine, die für die Regulation der Redox-Homöostase in der Zelle verantwortlich sind. Ein Funktionsverlust dieser Proteine durch die kovalente Bindung reaktiver Furan-Metabolite könnte eine verminderte Fähigkeit der Zelle oxidativen Stress abzuwehren zur Folge haben, was wiederum zum Zelltod führen könnte. Zusätzlich dazu, dass die kovalente Modifikation mehrerer Proteine aus dem gleichen Stoffwechselweg dessen Gesamtfunktion beeinträchtigen kann, ist es außerdem möglich, dass Adduktbildung an einzelnen Proteinen mit Schlüsselfunktionen in der Aufrechterhaltung der Zellhomöostase toxische Effekte auslösen kann. Ein Funktionsverlust dieser Proteine, die z.B. in Transportprozesse durch Mitochondrienmembranen, zelluläre Signalwege, DNA-Methylierung, Blutgerinnung und Gallensäuren-Transport involviert sind, könnte ebenfalls an den zytotoxischen und kanzerogenen Wirkungen von Furan beteiligt sein. Die kovalente Bindung reaktiver Furan-Metabolite an zelluläre Proteine kann zu einer Akkumulation großer Mengen an ungefalteten oder beschädigten Proteinen im endoplasmatischen Retikulum (ER) führen. Als Antwort auf diesen sogenannten ER-Stress kann die Zelle den Unfolded Protein Response (UPR) aktivieren, einen zellulären Signalweg um vermehrt beschädigte Proteine zu reparieren oder abzubauen. Um festzustellen, ob die Bindung reaktiver Furan-Metabolite an zelluläre Proteine eine Aktivierung des UPR auslöst, wurden semiquantitative PCR und Real-Time-PCR Analysen durchgeführt. Nach einer Aktivierung des UPR sollte...
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Accuracy of furan analysis in estimating the degree of polymerization in power transformersMtetwa, Nkosenye Sidwell 16 September 2011 (has links)
MSc (Eng), School of Electrical and Information Engineering, Faculty of Engineering and the Built Environment
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Synthesis and Characterization of Polymeric Schiff Bases from 2,5-DiformylfuranXiang, Tengfei 20 December 2012 (has links)
No description available.
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