2015
DOI: 10.1016/j.saa.2014.10.102
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Fluorescence quenching of 7-amino-4-methylcoumarin by different TEMPO derivatives

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Cited by 26 publications
(14 citation statements)
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“…In addition, degradation or metabolization of compounds during their incubation with the E. coli detection culture could affect their fluorescent properties. To assess such potential effects (which clearly must be distinguished and accounted for) we investigated the interference caused by the model fluorescent compound 7-amino-4-methylcoumarin (7-AMC) and fluorescence-quenching compound rifampicin (Richter et al, 2015; Żamojć et al, 2015). As anticipated, these compounds respectively increased and decreased fluorescence recorded in the assay ( Figure 5 ).…”
Section: Resultsmentioning
confidence: 99%
“…In addition, degradation or metabolization of compounds during their incubation with the E. coli detection culture could affect their fluorescent properties. To assess such potential effects (which clearly must be distinguished and accounted for) we investigated the interference caused by the model fluorescent compound 7-amino-4-methylcoumarin (7-AMC) and fluorescence-quenching compound rifampicin (Richter et al, 2015; Żamojć et al, 2015). As anticipated, these compounds respectively increased and decreased fluorescence recorded in the assay ( Figure 5 ).…”
Section: Resultsmentioning
confidence: 99%
“…Photoluminescence emission (PL) spectrum was obtained on a fluorescence spectrophotometer (Hitachi, F4600) at the scope of 400–600 nm with a photomultiplier tube handled at 800 volt. A 150 watt xenon lamp was served as the pumping source, at an excitation wavelength of 340 nm (Zamojć et al, 2015 ). The emission and excitation slits size were 5 nm and scan speed was setting at 240 nm per min.…”
Section: Methodsmentioning
confidence: 99%
“…We wanted to show (in comparison to our earlier investigations) that the affinity of the peptides to metal ions depends not only on the primary structure (amino acid composition) but also -to a large extent -on the shape of the adopted peptide conformation. We report herein the type of interactions between the peptide fragment of the Aβ polypeptide, Aβ (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16) : Ac-Arg-His-AspSer-Gly-Tyr-Glu-Val-His-His-Gln-Lys-NH 2 hereafter referred to as HZ1, and Cu 2+ ions.…”
Section: Introductionmentioning
confidence: 99%
“…The studies on the fluorescence quenching performed in our group with the use of steady state and transient methods provided a large quantity of information, mainly about fluorescent dyes [12][13][14][15]. Additionally, such a technique has been widely used for acquiring qualitative and quantitative information on peptides containing fluorescent amino acids (tyrosine, phenylalanine and tryptophan) as quenched by paramagnetic metal ions (Mn 2+ , Co 2+ , Cu 2+ ) [11,[16][17][18][19][20].…”
Section: Introductionmentioning
confidence: 99%