Relevant bibliographies by topics / Tryptophol

Academic literature on the topic 'Tryptophol'

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Published: 10 March 2023

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Journal articles on the topic "Tryptophol"

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Wu, Ju, Hussein Abou-Hamdan, Régis Guillot, Cyrille Kouklovsky, and Guillaume Vincent. "Electrochemical synthesis of 3a-bromofuranoindolines and 3a-bromopyrroloindolines mediated by MgBr2." Chemical Communications 56, no. 11 (2020): 1713–16. http://dx.doi.org/10.1039/c9cc09276e.

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Palmieri, Alessandro, and Marino Petrini. "Tryptophol and derivatives: natural occurrence and applications to the synthesis of bioactive compounds." Natural Product Reports 36, no. 3 (2019): 490–530. http://dx.doi.org/10.1039/c8np00032h.

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This report presents some fundamental aspects related to the natural occurrence and bioactivity of tryptophol as well as the synthesis of tryptophols and their utilization for the preparation of naturally occurring alkaloid metabolites embedding the indole system.
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Kosalec, Ivan, Snježana Ramić, Dubravko Jelić, Roberto Antolović, Stjepan Pepeljnjak, and Nevenka Kopjar. "Assessment of Tryptophol Genotoxicity in Four Cell Lines In Vitro: A Pilot Study with Alkaline Comet Assay." Archives of Industrial Hygiene and Toxicology 62, no. 1 (March 1, 2011): 41–49. http://dx.doi.org/10.2478/10004-1254-62-2011-2090.

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Assessment of Tryptophol Genotoxicity in Four Cell LinesIn Vitro: A Pilot Study with Alkaline Comet AssayTryptophol is an aromatic alcohol and secondary metabolite of the opportunistic fungusCandida albicans. Although its toxicity profile at cell level has been poorly investigated, recent data point to cytotoxic, cytostatic, and genotoxic effects in lymphocytes and the induction of apoptosis in leukaemic blood monocytes. In this pilot study we evaluated the genotoxicity of tryptopholin vitroon four permanent cell lines of animal and human origin: ovary cells, alveolar epithelium, liver cells, and blood monocytes using the alkaline comet assay. We selected cells that might be principal targets of tryptophol and other low-molecular geno(toxins) secreted byCandida albicansduring host invasion. Our results suggest that tryptophol appliedin vitroat 2 mmol L-1for 24 h damages DNA in HepG2, A549 and THP-1 cells, obviously due to bioactivation and/or decomposition of the parent compound, which results in the formation of more genotoxic compound(s) and production of reactive species that additionally damage DNA. On the other hand, notably lower levels of primary DNA damage were recorded in CHO cells, which lack metabolic activity. Future studies with tryptophol should look further into mechanisms involved in its toxic action and should focus on other cell types prone to infection withCandidaspp. such as vaginal epithelial cells or keratinocytes of human origin.
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WONGSUK, Thanwa, and Passanesh SUKPHOPETCH. "Effect of Quarum Sensing Molecules on Aspergillus fumigatus." Walailak Journal of Science and Technology (WJST) 17, no. 4 (April 19, 2019): 348–58. http://dx.doi.org/10.48048/wjst.2020.6172.

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Aspergillus fumigatus is an opportunistic fungal pathogen to which immunocompromised patients are especially susceptible. A. fumigatus can form biofilms both in vitro and in vivo. Quorum sensing molecules (QSMs) have activity against some fungi. This study aimed to determine the activity of the QSMs farnesol, tyrosol, phenylethanol and tryptophol against the growth A. fumigatus on solid media, and against its ability to form biofilms. The activity of each QSM against planktonic A. fumigatus growth was assessed using the CLSI M38-A2 broth microdilution assay, while QSM inhibition of A. fumigatus’s biofilm formation was measured in crystal violet, and 2, 3-bis (2-methoxy-4-nitro-5-sulfo-phenyl)-2H-tetrazolium-5-caboxanilide (XTT) assays. The QSMs reduced the colony diameter of the studied strains in a QSM-dependent pattern. Tryptophol showed the best effect and tyrosol showed the poorest effect. The minimum inhibitory concentrations (MICs) for farnesol, tyrosol, phenylethanol and tryptophol tested against A. fumigatus were > 32, > 32, 16 and 8 mM, respectively. The effective concentration each QSM required to inhibit A. fumigatus biofilm formation were higher than the planktonic MICs. In this study, the performance of QSMs against A. fumigatus ranked from best to worst as follows: tryptophol, phenylethanol, farnesol and tyrosol. Because of phenylethanol and tryptophol showed the strongest effect to the growth and biofilm formation of A. fumigatus. Therefore, the cytotoxic activities of phenylethanol and tryptophol in A549 cells (lung alveolar epithelial cells) were determined. However, phenylethanol and tryptophol induced A549 cell damage (at MIC level), as demonstrated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium (MTT) and lactate dehydrogenase (LDH) assays.
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Khedkar, Vivek, Annegret Tillack, Manfred Michalik, and Matthias Beller. "Convenient synthesis of tryptophols and tryptophol homologues by hydroamination of alkynes." Tetrahedron 61, no. 32 (August 2005): 7622–31. http://dx.doi.org/10.1016/j.tet.2005.05.093.

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Cordente, Antonio G., Damian Espinase Nandorfy, Mark Solomon, Alex Schulkin, Radka Kolouchova, Ian Leigh Francis, and Simon A. Schmidt. "Aromatic Higher Alcohols in Wine: Implication on Aroma and Palate Attributes during Chardonnay Aging." Molecules 26, no. 16 (August 17, 2021): 4979. http://dx.doi.org/10.3390/molecules26164979.

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The higher alcohols 2-phenylethanol, tryptophol, and tyrosol are a group of yeast-derived compounds that have been shown to affect the aroma and flavour of fermented beverages. Five variants of the industrial wine strain AWRI796, previously isolated due to their elevated production of the ‘rose-like aroma’ compound 2-phenylethanol, were characterised during pilot-scale fermentation of a Chardonnay juice. We show that these variants not only increase the concentration of 2-phenylethanol but also modulate the formation of the higher alcohols tryptophol, tyrosol, and methionol, as well as other volatile sulfur compounds derived from methionine, highlighting the connections between yeast nitrogen and sulfur metabolism during fermentation. We also investigate the development of these compounds during wine storage, focusing on the sulfonation of tryptophol. Finally, the sensory properties of wines produced using these strains were quantified at two time points, unravelling differences produced by biologically modulating higher alcohols and the dynamic changes in wine flavour over aging.
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Xu, Jun, and Rongbiao Tong. "An environmentally friendly protocol for oxidative halocyclization of tryptamine and tryptophol derivatives." Green Chemistry 19, no. 13 (2017): 2952–56. http://dx.doi.org/10.1039/c7gc01341h.

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Gu, Quanli, Swarna Basu, and J. L. Knee. "Tryptophol Cation Conformations Studied with ZEKE Spectroscopy." Journal of Physical Chemistry A 111, no. 10 (March 2007): 1808–13. http://dx.doi.org/10.1021/jp067355a.

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Guzmán-López, Oswaldo, Ángel Trigos, Francisco J. Fernández, María de Jesús Yañez-Morales, and Gerardo Saucedo-Castañeda. "Tyrosol and tryptophol produced by Ceratocystis adiposa." World Journal of Microbiology and Biotechnology 23, no. 10 (April 25, 2007): 1473–77. http://dx.doi.org/10.1007/s11274-007-9392-9.

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Laćan, Goran, Volker Magnus, Šumski Šimaga, Sonja Iskrić, and Prudence J. Hall. "Metabolism of Tryptophol in Higher and Lower Plants." Plant Physiology 78, no. 3 (July 1, 1985): 447–54. http://dx.doi.org/10.1104/pp.78.3.447.

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Dissertations / Theses on the topic "Tryptophol"

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Lara, Maria Cristina Figueiredo Lima e. "Estudos das interações do íon Cu2+ com os dipeptídeos glicil-triptofano e triptofil-glicina." Universidade de São Paulo, 1993. http://www.teses.usp.br/teses/disponiveis/54/54132/tde-25022014-114118/.

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Neste trabalho, são estudados dois dipeptídeos complexados com cobre, Triptofil-Glicina (trp-Gly) e Glicil-Triptofano (Gly-Trp). Focalizamos a interação com o metal de transição, mudanças conformacionais, papel do resíduo pesado de triptofano na simetria dos complexos formados, e explicamos as propriedades espectroscópicas atípicas que observamos no Gly-Trp: Cu+2 em pH´s altos semelhantes aquelas apresentadas em uma espécie de proteínas naturalmente complexadas as proteínas azuis. Para atingirmos tais objetivos, lançamos mão das técnicas de RPE, Dicroísmo Circular (CD) e Absorção ótica, pelas suas complementaridades. Com os dados experimentais, propusemos dois modelos para os complexos com suas funções de onda. Para Trp-Gly: Cu+2, nos pH´s 9,1 e 13,2 e para o Gly-Trp: Cu+2 no pH= 9,1 propomos um modelo que chamamos de covalente. Que consiste basicamente em considerar que os orbitais do íon Cu+2 e seus ligantes, se encontram em simetria quadrado planar (D4h) e que cada ligante no caso nosso, dois oxigênios e dois nitrogênios, tem disponíveis seus orbitais 2s, 2px, 2py, 2pz para a formação dos orbitais moleculares com os orbitais 3d do cobre. As funções assim construídas, dependem de coeficientes que nos dão informações sobre o grau de covalência. O método é semi-empírico. As expressões teóricas dos parâmetros RPE dependem destes parâmetros de covalência e das energias de transição obtidas por absorção ótica no visível. Pudemos então com os valores experimentais das componentes dos tensores g e A obtermos os valores numéricos dos parâmetros de covalência. Para o complexo Gly-Trp: Cu+2, no pH=13,2, propusemos o modele de mistura de orbitais, um modele não covalente que consiste em considerarmos as funções de onda dos estados excitados 4s e 4p do cobre misturadas com as dos orbitais 3d do mesmo íon, para explicar as propriedades espectroscópicas pouco comuns, que se deslocam na direção daquelas obtidas nas proteínas azuis. Conhecendo os valores experimentais das componentes dos tensores g e A, da força de oscilador obtida dos espectros óticos e da força rotacional obtida dos espectros CD, e das auto-funções compatíveis com o modelo, determinamos numericamente os coeficientes de hibridização (mistura). Os parâmetros experimentais, foram determinados através de simulações espectrais, utilizando programas desenvolvidos para este fim. Através deste trabalho, pudemos enfim, verificar a influência do resíduo pesado de triptofano na estereoquímica dos complexos formados, mudanças de simetria, o caráter das ligações, e ate que ponto as propriedades do dipeptídeo Gly- Trp: Cu2+ em pH alto, são semelhantes às proteínas azuis
In this work we studied two dipeptide-copper complexes, being Triptofil-Glycine (Trp-Gly) and Glycil-Triptophan (Gly-Trp). We focused our interest on the interaction with the transition metal, conformational changes and the role that the heavy residue of the Triptophan plays in the symmetry of the complex. Moreover we explain the unusual spectroscopic properties that we observed with Gly-Trp: Cu+2 in high pH solutions similar to that of the so called blue proteins. For these purposes we used such complementary techniques as EPR, Circular Diochrism and Optical Absorption Spectroscopy. Based on our experimental results we proposed two models for the complexes and their wave functions. For the TRP-Gly: Cu+2 in pH of 9.1 and 13.2 and for Gly-Trp: Cu+2 with pH=9.1, we use a model which we call covalent. It consists basically of the consideration that the electronic orbital of the ion Cu+2 and its ligands are in square planar symmetry and that each of the four ligand atoms, in our case two oxygen and two nitrogen atoms, has available 2s, 2px, 2py, 2pz for the formation of molecular orbital with the copper 3d orbital. The wave functions thus constructed depend on coefficients (parameters) that give information on the degree of the covalent character of the bond (complex). The method is semi-empirical. The theoretical expressions for the EPR parameters depend on these coefficients and the transition energies obtained by absorption spectroscopy (in the visible). With the experimental values of the g and A tensors we can therefore obtain numerical values for the covalent coefficients. For the complex Gly-Trp: Cu+2 with pH=13.2 we proposed a model of mixing orbital, a non covalent model that consists of the assumption that the wave functions of the excited states 4s and 4p of the copper mix with the 3d orbital of the same ion. With this model it was possible to explain the uncommon spectroscopic properties that are similar to these of the blue proteins. Knowing the experimental values of the components of the tensors g and A, the oscillator strength obtained by the optical spectra, the rotational strength obtained by the CD spectra and the eigen-functions compatible with the model, we numerically determined the coefficients of hybridization. The experimental parameters were determined by spectral simulations using programs that we developed especially (specifically) for this purpose. Trough this work it was possible to verify the influence of Triptophan on the stereochemistry (stereo chemical behavior) of the formed complexes, on symmetry changes, covalent character and up to which point the properties of the dipeptide Gly-Trp: Cu+2 in high pH are similar to that of the blue protein
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Fu, Rong. "Biochemical and Spectroscopic Characterization of Tryptophan Oxygenation: Tryptophan 2, 3-Dioxygenase and Maug." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_diss/44.

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TDO utilizes b-type heme as a cofactor to activate dioxygen and insert two oxygen atoms into free L-tryptophan. We revealed two unidentified enzymatic activities of ferric TDO from Ralstonia metallidurans, which are peroxide driven oxygenation and catalase-like activity. The stoichiometric titration suggests that two moles of H2O2 were required for the production of one mole of N-formylkynurenine. We have also observed monooxygenated-L-tryptophan. Three enzyme-based intermediates were sequentially detected in the peroxide oxidation of ferric TDO in the absence of L-Trp including compound I-type and compound ES-type Fe-oxo species. The Fe(IV) intermediates had an unusually large quadrupole splitting parameter of 1.76(2) mm/s at pH 7.4. Density functional theory calculations suggest that it results from the hydrogen bonding to the oxo group. We have also demonstrated that the oxidized TDO was activated via a homolytic cleavage of the O-O bond of ferric hydroperoxide intermediate via a substrate dependent process to generate a ferrous TDO. We proposed a peroxide activation mechanism of the oxidized TDO. The TDO has a relatively high redox potential, the protonated state of the proximal histidine upon substrate binding as well as a common feature of the formation of ferric hydroxide species upon substrate or substrate analogues binding. Putting these together, we have proposed a substrate-based activation mechanism of the oxidized TDO. Our work also probed the role of histidine 72 as an acid-base catalyst in the active site. In H72S and H72N mutants, one water molecule plays a similar role as that of His72 in wild type TDO. MauG is a c-type di-heme enzyme which catalyze the biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. Its natural substrate is a monohydroxylated tryptophan residue present in a 119-kDa precursor protein of methylamine dehydrogenase (MADH). We have trapped a novel bis-Fe(IV) intermediate from MauG, which is remarkably stable. A tryptophanyl radical intermediate of MADH has been trapped after the reaction of the substrate with the bis-Fe(IV) intermediate. Analysis by high-resolution size-exclusion chromatography shows that MauG can tightly bind to the biosynthetic precursor and form a stable complex, but the mature protein substrate does not.
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Walsh, Harold Archibold. "Regulation of tryptophan-2,3-dioxygenase and pineal indoleamines by selected tryptophan derivatives and antidepressants." Thesis, Rhodes University, 1997. http://hdl.handle.net/10962/d1004077.

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The regulation of tryptophan-2,3-dioxygenase (TDO) (EC 1.13.1.12) and, to a lesser extent, pineal indoleamines, both in vitro and in vivo, is examined in this study. Rat liver TDO is a cytosolic enzyme which plays a crucial role in the regulation of circulating tryptophan (TRP) levels. Stimulation of this enzyme by heme enhances the catabolism of TRP, making less TRP available for uptake into the brain and other tissues, and for protein synthesis. At pH 7, the enzyme has an approximate Km of 100μM, is subject to substrate inhibition immediately beyond Sopt([S] at Vmax), and response of the enzyme is cooperative in both uninhibited and inhibited regions. Hill analysis of the uninhibited region reveals a biphasic plot and two classes of binding sites. Negative cooperativity is brought about through deprotonation of the enzyme. Substrate iphibition also occurs at both acidic and basic pH values with concomitant shifts in Sopt. The results obtained indicate that substrate inhibition could be an additional mechanism whereby the flux through the TRP-kynurenine pathway is regulated. TDO is subject to a diurnal rhythm, with peak activity during the pre-dark period and the loweSt activity towards the end of the dark period. It is possible that the enzyme controls the synthesis of the neurotransmitter serotonin (5-HT), and that the circadian rhythm in TDO activity is due to the endogenous rhythm of melatonin (aMT) production by the pineal gland. In the present study, aMT displaces TRP from bovine serum albumin (BSA) in vitro, and it is therefore possible for the indoleamine to regulate the availability of TRP for uptake into the brain for conversion to its derivatives. Chronic intraperitoneal administration of aMT affects physiological hepatic parameters in rats, such as TDO activity and stromal fatty acid composition, whilst no observable effect is demonstrable with respect to protein synthesis, nucleic acid metabolism, membrane fatty acid composition and pineal indole biosynthesis. On the other hand, chronic treatment of rats with antidepressants, the tricyclic desmethylimipramine (DMI) and the selective serotonin reuptake inhibitor (SSRI), fluoxetine, reveals significant negative alterations in TDO concentrations and pineal indole amine synthesis. Combining aMT with any of these two drugs normalises the activity of the hepatic enzyme. DMI is found to be an effective inhibitor of TDO in the micromolar range in vitro, and also affects total enzyme concentrations in vivo. Fluoxetine has no effect on TDO in vitro, but in vivo also reduces total enzyme levels in the liver. However, the SSRI does not affect conjugation between apo- and holoenzyme. Instead, it decreases extant holoenzyme levels. Indoleamine synthesis by the pineal gland, in organ culture, is altered by both antidepressants, although in different ways. DMI increases N-acetylserotonin levels and reduces the output of methoxyindole acetic acid and meth6xytryptophol. Fluoxetine treatment markedly reduces aMT concentrations and also brings about high levels of the 5-HT catabolites, 5-hydroxytryptophol and 5-hydroxyindole acetic acid. Insulin also lowers aMT synthesis significantly in pineal organ cultures, via a mechamsm that involves inhibition of the enzyme, N-acetyl transferase, that regulates aMT synthesis. The effects of insulin on pineal indole metabolism are due to the observation that a carbohydrate rich diet which induces insulin release elevates plasma TRP and brain 5-HT, but has no effect on pineal TRP and indole amine synthesis. It could thus be possible for insulin to have an effect on the pineal, since the latter is outside the blood brain barrier. The finilings of this study support the biogenic amine deficiency hypothesis, implicating some of the major biogenic amines such as noradrenaline (NA), 5-HT and aMT in depression. There is believed to be a deficiency of NA and 5-HT at their respective synapses in the depressed state. The drug DMI could act, firstly, by inhibiting TDO and thus increasing plasma TRP levels, and could, secondly, stimulate NA release and inhibit NA reuptake at the pineal membrane. The combined effect would be to enhance aMT synthesis, with eventual remission. Fluoxetine, on the other hand, appears to utilize a slightly different mode of action to DMI, which seems to focus on the preservation of 5-HT. The fact that aMT counteracts the effects of both antidepressants, and restores the activity of TDO to that of the controls, is also consistent with the observation that the therapeutic action of drugs such as these coincides willi the restoration of normal plasma levels of the neurohormone in depressives. In view of the biogenic amine deficiency hypothesis of depression and the contentious claim that TDO is the major peripheral determinant of brain TRP, brain 5-HT and ultimately aMT, the regulation of TDO is investigated and discussed. The study concludes that TDO activity is regulated by a number of endogenous compounds which are mainly derivatives of TRP, such as aMT and oxidized nicotinamide adenine dinucleotide and exogenous substances, of which DMI and fluoxetine are but two. In addition, modulation of IDO activity in depression appears to be an important aspect of antidepressant action. aMT, the product of the pineal gland, also has the potential to increase plasma TRP and hence forebrain TRP levels, and ultimately 5-HT concentrations, firstly by displacing TRP from serum albumin and secondly by inhibiting TDO.
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Brnardic, Edward Joseph. "Synthesis of aza-tryptophan derivatives." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0013/MQ52518.pdf.

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Schaechter, Judith Diane. "Tryptophan availability modulates serotonin release." Thesis, Massachusetts Institute of Technology, 1989. http://hdl.handle.net/1721.1/13995.

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Tsimpos, Kleomenis. "Τοwards a Synthetic Tryptophan Aminotransferase." Thesis, Linnéuniversitetet, Institutionen för kemi och biomedicin (KOB), 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-97548.

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The synthesis and evaluation of a molecularly imprinted polymer has been undertaken using an oxazine-based tryptophanamide transition state analogue (TSA) as template. An efficient route to the synthesis of oxazine-based TSAs for the reaction of pyridoxamine and indole-3-pyruvic acid has been established, with yields of up to 80%. NMR titration studies were performed to examine the interactions between the functional monomer, methacrylic acid and the template. Complexation of the template by functional monomer in the presence of crosslinker showed an apparent KD of 0.63-0.79 ± 0.04 M (293 K, acetonitrile-d3) based upon the chemical shift of the template amide protons. TSA-imprinted and non-imprinted reference polymers were synthesized by free radical polymerization in acetonitrile. Polymer monoliths were ground and fractionated into a 25-63 μm size range. Polymer-ligand recognition studies were conducted using the polymers as HPLC stationary phases. An imprinting factor (IF) of 2.93 was observed for the TSA, indicating the selectivity of the imprinted sites for the template. Studies using the D- and L-enantiomers of the phenylalaninamide analogue of the template showed enantioselectivity in the case of the imprinted polymer, α = 1.10, though not in the case of the non-imprinted reference polymer (1.00). Using UV-spectroscopy based polymer-ligand binding studies, a maximum theoretical capacity (Bmax) of 0.059 ± 0.004 mmol·g-1 was observed for the imprinted polymer. Conclusively, an imprinted polymer with binding sites selective for the TSA was successfully prepared and shall subsequently be studied with respect to its capacity to catalyse the transamination reaction between pyridoxamine and indole-3-pyruvic acid to yield pyridoxal and tryptophan.
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Mirzaei, Hamid. "Synthesis of tryptophan amides and lavendamycin analogs." Virtual Press, 2001. http://liblink.bsu.edu/uhtbin/catkey/1221298.

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The synthesis of 7-N-acetyl-3'-demethyllavendamycin propyl ester (61 ), 7-N-butr-3'-demethyllavendamycin amide of N,N-dimethylethylenediamine (62), 7-N-acetyllavendamycin butyl amide (64), 7-N- acetyllavendamycin amide of ethanolamine (63) are described. Incorporation of the Pictet-Spengler condensation of 7acetamido-2-formylquinoline-5, 8-dione (32) or 7-butyramido-2-formylquinoline-5, 8dione (7) with tryptophan propyl ester (65), L-tryptophan amide of N, N dimethylethylenediamine (66), f3-methyltryptophan butyl amide (68), or methyltryptophan amide of ethanolamine (67) in xylene afforded four lavendamycin analogs.Aldehydes 32, 74 and 86 were prepared according to the following general procedure. Nitration of 8-hydroxy-2-methylquinoline (69) yielded 8-hydroxy-2-methyl - 5,7-dinitroquinoline (29). Compound 29 was then hydrogenated and acylated with acetic anhydride or butyric anhydride or 2-furoyl chloride followed by hydrolysis to yield 5,7diacetamido-8-hydroxy-2-methylquinoline (75) or 5,7- dibutyramido-8- hydroxy-2methylquinoline (73) or 5,7-difuroylamino-8-hydroxy-2- methylquinoline (84). Compounds 75 and 73 and 84 were oxidized by potassium dichromate to give the corresponding 5,8-diones 31 or 72 or 85. Treatment of 31 or 72 or 85 with selenium dioxide in refluxing 1,4-dioxane afforded compounds 32 and 74 and 86, respectively.Tryptophan propyl ester (65) was synthesized via a Fischer esterification of Ltryptophan with propyl alcohol saturated with hydrogen chloride. Compounds 66, 67, 68, 76, 77, 78, 79, and 80 were synthesized via the conversion of esters to amides with dimethylaluminum amides. Tryptophan methyl ester (23) and (3-methyltryptophan methylester (11) were treated with premixed trimethylaluminum and primary amines and refluxed to afford the desired tryptophan and (3-methyltryptophan amides.The structures of the novel compounds 61, 62, 63, 64, 66, 67, 68, 76, 77, 78, 79, 80, were confirmed through 1H NMR, IR, EIMS, and HRMS. Elemental analyses of Compounds 66, 68, 76, 77, 78 and 80 were also included. 1H NMR and IR for known compounds 29, 30, 31, 32, 71, 73, 74, 75, 84, 85, 86 were provided also.
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Bergqvist, Peter B. F. "Tryptophan-related neurotransmission in the brain disturbances associated with experimental hepatic encephalopathy /." Lund : Dept. of Clinical Pharmacology, Institute of Labortaory Medicine, Lund University Hospital, 1997. http://catalog.hathitrust.org/api/volumes/oclc/39761954.html.

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Müller, Burkhardt. "Synthese, Analytik und Bildungsbedingungen von Kontaminanten in biotechnologisch hergestelltem Tryptophan." [S.l. : s.n.], 1999. http://deposit.ddb.de/cgi-bin/dokserv?idn=957463723.

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Solle, Dörte. "Analyse und Optimierung eines industriellen Biotransformationsprozesses zur Herstellung von Tryptophan." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969294492.

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Books on the topic "Tryptophol"

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Porter, Donna Viola. L-tryptophan: Health problems, production and regulatory status : proceedings of a CRS seminar. [Washington, D.C.]: Congressional Research Service, Library of Congress, 1991.

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Huether, Gerald, Walter Kochen, Thomas J. Simat, and Hans Steinhart, eds. Tryptophan, Serotonin, and Melatonin. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4709-9.

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Astin, Felicity. Huntington's disease and tryptophan metabolism. [Guildford]: Universityof Surrey, 1994.

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Filippini, Graziella Allegri, Carlo V. L. Costa, and Antonella Bertazzo, eds. Recent Advances in Tryptophan Research. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0381-7.

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Tryptophan: Biochemical and health implications. Boca Raton: CRC Press, 2002.

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Pollack, Robert L. The pain-free tryptophan diet. New York, NY: Warner Books, 1986.

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Allegri, Graziella, Carlo V. L. Costa, Eugenio Ragazzi, Hans Steinhart, and Luigi Varesio, eds. Developments in Tryptophan and Serotonin Metabolism. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0135-0.

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1932-, Allegri Graziella, ed. Developments in tryptophan and serotonin metabolism. New York: Kluwer Academic/Plenum, 2003.

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1932-, Allegri Graziella, and International Study Group for Tryptophan Research. Meeting, eds. Developments in tryptophan and serotonin metabolism. New York: Kluwer Academic/Plenum, 2003.

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Whitley, Blake L. Tryptophan: Dietary sources, functions, and health benefits. Hauppauge, N.Y: Nova Science Publishers, 2011.

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Book chapters on the topic "Tryptophol"

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Bährle-Rapp, Marina. "Tryptophan." In Springer Lexikon Kosmetik und Körperpflege, 569. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_10807.

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Kobayashi, Kensei. "Tryptophan." In Encyclopedia of Astrobiology, 1713. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1619.

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Benkert, Otto, Ion Anghelescu, Christoph Fehr, Gerhard Gründer, Philip Heiser, Christoph Hiemke, Christian Lange-Asschenfeldt, et al. "Tryptophan." In Pocket Guide Psychopharmaka von A bis Z, 251–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01910-4_113.

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Sewell, A. C. "Tryptophan." In Springer Reference Medizin, 2375. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3132.

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Turiault, Marc, Caroline Cohen, Guy Griebel, David E. Nichols, Britta Hahn, Gary Remington, Ronald F. Mucha, et al. "Tryptophan." In Encyclopedia of Psychopharmacology, 1347–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1754.

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Kobayashi, Kensei. "Tryptophan." In Encyclopedia of Astrobiology, 2556–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1619.

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Sewell, A. C. "Tryptophan." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_3132-1.

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Volkmar, Fred R. "Tryptophan." In Encyclopedia of Autism Spectrum Disorders, 1. New York, NY: Springer New York, 2020. http://dx.doi.org/10.1007/978-1-4614-6435-8_1842-3.

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Campbell, Daniel, Corey Ray-Subramanian, Winifred Schultz-Krohn, Kristen M. Powers, Renee Watling, Christoph U. Correll, Stephanie Bendiske, et al. "Tryptophan." In Encyclopedia of Autism Spectrum Disorders, 3189. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1698-3_1842.

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Colzato, Lorenza S., Ana Beatriz Rodríguez Moratinos, Martin Reuter, and Peter Kirsch. "Tryptophan." In Theory-Driven Approaches to Cognitive Enhancement, 17–29. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57505-6_2.

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Conference papers on the topic "Tryptophol"

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McCaul, Colin, and Richard D. Ludescher. "Phosphorescence from tryptophan and tryptophan analogs in the solid state." In BiOS '98 International Biomedical Optics Symposium, edited by Joseph R. Lakowicz and J. B. Alexander Ross. SPIE, 1998. http://dx.doi.org/10.1117/12.307068.

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Bian, Qiyu, and Jiamei Wang. "Tryptophan hydroxylase 2 and tryptophan mediate depression by regulating serotonin levels." In 4TH INTERNATIONAL CONFERENCE ON FRONTIERS OF BIOLOGICAL SCIENCES AND ENGINEERING (FBSE 2021). AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0096466.

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Sanz, M., José Alonso, Santiago Mata, and Carlos Cabezas. "ROTATIONAL SPECTRUM OF TRYPTOPHAN." In 69th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2014. http://dx.doi.org/10.15278/isms.2014.td04.

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Bohora, Sanket, Kezheng Li, Prashant Waiba, Sishir Gautam, Augusto Martins, Ricardo A. Rodrigues, Peter Kikstra, et al. "A Low-cost Fresnel Lens Fluorometer to Detect Fecal Contamination in Drinking Water in Realtime." In CLEO: Applications and Technology. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/cleo_at.2022.am5m.8.

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We report the detection of tryptophan at sub-ppb levels for a fluorometer based on Fresnel lenses and low-cost electronics. These fluorometers can be used to detect fecal contamination in drinking water, indicated by tryptophan-like fluorescence.
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Petrich, J. W., J. W. Longworth, and G. R. Fleming. "Electron Transfer in Homologous Azurins." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.tuf7.

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Using time correlated single photon counting, we have studied electron transfer rates, kET in the homologous blue-copper proteins, azurins, obtained from Pseudomonas aeruginosa (Pae) and Alcaligenes faecalis (Afe). The salient difference between these proteins lies in the position of their single tryptophan residues. The tryptophan in azurin Pae, W48, is buried in the hydrophobic core of the protein while the tryptophan in azurin Afe, W118, lies on the protein surface, exposed to the solvent [1]. kET for the reaction W* + Az-Cu (II)→W*+·+Az-Cu(I) was determined to be 1 × 1010 s−1 and 0.5 × 1010s−1 for Pae and Afe, respectively ; i.e. kET(W48)/kET(W118) = 2.
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Barkley, Mary D., Luanne F. Tilstra, Lloyd P. McMahon, Marco A. Vela, and Mark L. McLaughlin. "Photophysics of constrained tryptophan derivatives." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Joseph R. Lakowicz. SPIE, 1990. http://dx.doi.org/10.1117/12.17693.

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Hu, Yi, Jean M. MacInnis, Binny J. Cherayil, Graham R. Fleming, Karl F. Freed, and Angelo Perico. "Dynamics studies of tryptophan and single tryptophan containing peptides: simulations and an analytical model." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Joseph R. Lakowicz. SPIE, 1990. http://dx.doi.org/10.1117/12.17707.

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Sordillo, Laura A., Peter P. Sordillo, Lin Zhang, and Robert R. Alfano. "Tryptophan and kynurenines in neurodegenerative disease." In Bio-Optics: Design and Application. Washington, D.C.: OSA, 2019. http://dx.doi.org/10.1364/boda.2019.jt4a.8.

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Schlamadinger, Diana E., Hannah S. Shafaat, Katheryn M. Sanchez, Jonathan E. Gable, Judy E. Kim, P. M. Champion, and L. D. Ziegler. "Tryptophan Residues as Membrane Protein Anchors." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482447.

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Sattler, Melissa C., William R. Cherry, and Mary D. Barkley. "Constrained Tryptophan Has A Monoexponential Decay." In 1988 Los Angeles Symposium--O-E/LASE '88, edited by Joseph R. Lakowicz. SPIE, 1988. http://dx.doi.org/10.1117/12.945389.

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Reports on the topic "Tryptophol"

1

Wirtman, Richard J. Tyrosine, Tryptophan and Performance. Fort Belvoir, VA: Defense Technical Information Center, December 1992. http://dx.doi.org/10.21236/ada266278.

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Spek, J. W. Standardized ileal digestible tryptophan requirement for broilers. Wageningen: Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/455515.

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Spek, J. W. Standardized ileal digestible tryptophan requirement for laying hens. Wageningen: Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/455522.

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Woolley, G. A., and B. A. Wallace. Circular Dichroism Studies of Tryptophan Residues in Gramicidin. Fort Belvoir, VA: Defense Technical Information Center, January 1992. http://dx.doi.org/10.21236/adp008376.

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Schiffer, M., C. H. Chang, and F. J. Stevens. The functions of tryptophan residues in membrane proteins. Office of Scientific and Technical Information (OSTI), August 1994. http://dx.doi.org/10.2172/10172497.

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Mertz, Isaac, Nick Christians, Adam Thoms, Benjamin Pease, Erik Ervin, and Xunzhong Zhang. Creeping Bentgrass Responses to a Tryptophan-Containing Organic Byproduct. Ames: Iowa State University, Digital Repository, 2018. http://dx.doi.org/10.31274/farmprogressreports-180814-2046.

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Kellner, Trey A., Stacie A. Gold, Dean Koehler, Lynnea Courtney, Leah Gesing, and John F. Patience. Determination of SID Tryptophan to Lysine Ratio in Nursery Pigs. Ames (Iowa): Iowa State University, January 2017. http://dx.doi.org/10.31274/ans_air-180814-331.

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Bonnin, Alexandre, Nick Goeden, Brett Lund, and George Anderson. Altered Placental Tryptophan Metabolism: A Crucial Molecular Pathway for the Fetal Programming of Neurodevelopmental Disorders. Fort Belvoir, VA: Defense Technical Information Center, July 2014. http://dx.doi.org/10.21236/ada611000.

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Hatch, Duane M. synthesis of selenium- and tellurium-containing tryptophan analogs for the elucidation of protein structure and function. Office of Scientific and Technical Information (OSTI), August 2015. http://dx.doi.org/10.2172/1209470.

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Lu, Zhidong. Ovarian Steroid Regulation of Tryptophan Hydroxylase Enzyme Level in the Midbrain Raphe in Ovariectomized Guinea Pigs. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.7193.

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