Emission of Thioflavin T and its Off–On Control in Polymer Membranes‡¶

Raj, C. Retna; Ramaraj, Ramasamy

doi:10.1562/0031-8655(2001)074<0752:eottai>2.0.co;2

Cited by 31 publications

(39 citation statements)

References 29 publications

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“…In fibril-bound ThT, rotation around this bond would be prevented leading to increase in fluorescence quantum yield. Conversely, others have proposed that fluorescence quantum yield of ThT results from excimer formation (Groenning et al, 2007a;Raj and Ramaraj, 2001). The localization of the ThT-binding sites on the fibrils and the binding mode of ThT are also debated.…”

Section: Introductionmentioning

confidence: 99%

On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

Sabaté¹,

Lascu²,

Saupe³

2008

Journal of Structural Biology

105

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Section: Introductionmentioning

confidence: 99%

On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

Sabaté¹,

Lascu²,

Saupe³

2008

Journal of Structural Biology

105

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“…Antibodies have been found to be very specific for labeling of amyloid adhesins (32,47), whereas ThT suffers from some nonspecificity, since it can also bind to cellulose and DNA (19,51). As most bacteria in environmental biofilms are still uncultured, a combination of ThT or antibodies with fluorescence in situ hybridization (FISH) and oligonucleotide probes can be used to identify bacteria producing amyloid adhesins (32).…”

mentioning

confidence: 99%

Amyloid-Like Adhesins Produced by Floc-Forming and Filamentous Bacteria in Activated Sludge

Larsen

Nielsen

Otzen

et al. 2008

Appl Environ Microbiol

168

107

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Amyloid proteins (fimbriae or other microbial surface-associated structures) are expressed by many types of bacteria, not yet identified, in biofilms from various habitats, where they likely are of key importance to biofilm formation and biofilm properties. As these amyloids are potentially of great importance to the floc properties in activated sludge wastewater treatment plants (WWTP), the abundance of amyloid adhesins in activated sludge flocs from different WWTP and the identity of bacteria producing these were investigated. Amyloid adhesins were quantified using a combination of conformationally specific antibodies targeting amyloid fibrils, propidium iodide to target all fixed bacterial cells, confocal laser scanning microscopy, and digital image analysis. The biovolume fraction containing amyloid adhesins ranged from 10 to 40% in activated sludge from 10 different WWTP. The identity of bacteria producing amyloid adhesins was determined using fluorescence in situ hybridization with oligonucleotide probes in combination with antibodies or thioflavin T staining. Among the microcolony-forming bacteria, amyloids were primarily detected among Alpha-and Betaproteobacteria and Actinobacteria. A more detailed analysis revealed that many denitrifiers (from Thauera, Azoarcus, Zoogloea, and Aquaspirillum-related organisms) and Actinobacteria-related polyphosphate-accumulating organisms most likely produced amyloid adhesins, whereas nitrifiers did not. Many filamentous bacteria also expressed amyloid adhesins, including several Alphaproteobacteria (e.g., Meganema perideroedes), some Betaproteobacteria (e.g., Aquaspirillum-related filaments), Gammaproteobacteria (Thiothrix), Bacteroidetes, Chloroflexi (e.g., Eikelboom type 1851), and some foam-forming Actinobacteria (e.g., Gordonia amarae). The results show that amyloid adhesins were an abundant component of activated sludge extracellular polymeric substances and seem to have unexpected, divers functions.

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“…The chemical compositions of AgI NPs were analyzed by an energydispersive X-ray (EDX) spectrograph. 8,9,19 In order to illustrate the above fact, we monitored the fluorescence emission spectra of ThT with varied concentrations in solution. To demonstrate ThT@AgI SPs, we integrated Ag + , I with ThT and observed spontaneous formation of supraparticles.…”

Section: Resultsmentioning

confidence: 99%

Ratiometric fluorescence detection of silver ions using thioflavin T-based organic/inorganic hybrid supraparticles

Zhang

et al. 2015

Analyst

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In this work, we present a new type of functional organic/inorganic hybrid supraparticle that spontaneously assembles from silver ions (Ag(+)), iodide ions (I(-)) and thioflavin T (ThT) under aqueous solution conditions. ThT alone in aqueous solution was weakly fluorescent with an emission band at 494 nm, which was related to the monomer. However, in the above-mentioned hybrid supraparticle (i.e., ThT@AgI SP) structure, the ThT monomer can form a dimer with a new emission band. The new band shifted to 546 nm and the emission intensity increased. We further present a facile strategy of reversible fluorescence switching of ThT by a simple cation (Ag(+)) and anions (I(-) and S(2-)), which can be employed for the ratiometric fluorescence detection of Ag(+) with high sensitivity and selectivity. The linear range of detecting Ag(+) was from 100 nM to 10 μM, with a limit of detection as low as approximately 50 nM. Moreover, it can be successfully applied for the operation of a logic gate system and to the sensing of Ag(+) in real water samples.

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Emission of Thioflavin T and its Off–On Control in Polymer Membranes‡¶

Cited by 31 publications

References 29 publications

On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

Amyloid-Like Adhesins Produced by Floc-Forming and Filamentous Bacteria in Activated Sludge

Ratiometric fluorescence detection of silver ions using thioflavin T-based organic/inorganic hybrid supraparticles

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