The synthesis of some substituted macrocyclic ether-ester compounds

Thompson, M. D.; Bradshaw, Jerald S.; NIELSEN, S. F.; Bishop, Clark T.; COX, F. T.; Fore, P.E.; Maas, G.; Izatt, Reed M.; Christensen, James J.

doi:10.1016/0040-4020(77)80157-9

Cited by 33 publications

(1 citation statement)

References 18 publications

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“…Tiyocrown eterlerin makrohalkalı formasyonunun karbonil grubu kapsadığı önceden biliniyordu [28][29][30][31]. Makrosilik eter-ester bileşiğinin [32], eter-ester içeren geniş kapsamlı polieter-diester bileşiğinin [33][34][35][36][37][38][39][40], tiyoeter-ester [35,37,39,41] ve etertiyolester [35,37] bileşiğinin sentezi, Bradshaw, Izatt ve Christensen tarafından dibazik asit tuzu ve alfa, omega-dihalo bileşikleri veya dibazik asit klorürleri ve alfa, omegadihidroksi bileşiklerinden herhangi birine bağlanarak hazırlanmıştır. İki makrohalkalı polieter-monoester bileşikleri, Matsushima [42] tarafından normal verimlilikle bulunmuştur.…”

Section: Introductionunclassified

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Ergün¹,

Çiçek²

2018

Balıkesir Üniversitesi Fen Bilimleri Enstitüsü Dergisi

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Section: Introductionunclassified

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Ergün¹,

Çiçek²

2018

Balıkesir Üniversitesi Fen Bilimleri Enstitüsü Dergisi

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Synthesis of crown ethers and analogues

Weber

Toner

Goldberg

et al. 1989

PATAI'S Chemistry of Functional Groups

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Rapid Screening of Binding Constants by Calibrated Competitive ¹H NMR Spectroscopy

Heath

Dykes

Fish

et al. 2003

Chemistry A European J

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A calibrated competitive NMR method has been developed that is appropriate for the rapid screening of binding constants. This method involves the initial characterisation of a receptor-substrate binding event for which the (1)H NMR spectrum of a given receptor (calibrant) is modified by the substrate of interest at a range of concentrations. For all subsequent "unknown" receptors, K(a) values are then determined by using a competition assay (in the presence of the calibrant receptor) by measuring a single standard (1)H NMR spectrum. This enables a rapid assessment of the recognition properties of a library of potential receptors. Only the calibrant receptor needs to be NMR active, while the library of putative receptors, as well as the substrate, can be NMR silent. This method assumes the formation of complexes of 1:1 stoichiometry. To demonstrate this methodology, the binding of a number of crown ether type compounds with K+ ions has been studied. Comparison of the binding strengths obtained by using this approach with those in the literature shows excellent agreement. A range of new compounds that have recently been synthesised within our group has also been screened in order to illustrate how this approach can rapidly assess binding ability. This method has significance for chemists working in the fields of combinatorial receptor/substrate design and supramolecular chemistry as a means of rapid optimisation of binding strength.

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The synthesis of some substituted macrocyclic ether-ester compounds

Cited by 33 publications

References 18 publications

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Synthesis of crown ethers and analogues

Rapid Screening of Binding Constants by Calibrated Competitive ¹H NMR Spectroscopy

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The synthesis of some substituted macrocyclic ether-ester compounds

Cited by 33 publications

References 18 publications

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Investigation of the ınhibitory effects of some macrogenetic thiocrown ethers on polyphenol oxidase enzyme

Synthesis of crown ethers and analogues

Rapid Screening of Binding Constants by Calibrated Competitive 1H NMR Spectroscopy

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Rapid Screening of Binding Constants by Calibrated Competitive ¹H NMR Spectroscopy