2016
DOI: 10.1007/s00216-015-9271-4
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A facile and dynamic assay for the detection of peptide aggregation

Abstract: We report on a facile method to detect the aggregation and co-aggregation of peptides by tryptophan fluorescence spectroscopy. Peptide aggregates (PAs) play a pivotal role in neurodegenerative diseases, such as Alzheimer's and Parkinson's. The detection of the formation of aggregates, especially in the early stage, will facilitate the diagnosis and treatment of the associated disease. In this study, by choosing a tryptophan-containing peptide of EP2, we investigated its fluorescence spectroscopic characteristi… Show more

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Cited by 3 publications
(3 citation statements)
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“…To confirm this observation, the interaction between the bacterial membrane and C16‐KWKW was studied further by employing tryptophan fluorescence spectroscopic analysis (Caesar, Esbjorner, Lincoln, & Norden, ; Lin et al, ). In the fluorescence spectra, the amino acid tryptophan has a wavelength of maximum absorption of 280 nm and an emission peak ranging from approximately 300 to 350 nm depending on changes in the local environment.…”
Section: Resultsmentioning
confidence: 99%
“…To confirm this observation, the interaction between the bacterial membrane and C16‐KWKW was studied further by employing tryptophan fluorescence spectroscopic analysis (Caesar, Esbjorner, Lincoln, & Norden, ; Lin et al, ). In the fluorescence spectra, the amino acid tryptophan has a wavelength of maximum absorption of 280 nm and an emission peak ranging from approximately 300 to 350 nm depending on changes in the local environment.…”
Section: Resultsmentioning
confidence: 99%
“…To confirm this observation, the interaction between the bacterial membrane and C16-KWKW was further studied by employing tryptophan fluorescence spectroscopic analysis (Caesar, Esbjorner, Lincoln, & Norden, 2006;Lin et al, 2016). In the fluorescence spectra, the amino acid tryptophan has a wavelength of maximum absorption of 280 nm and an emission peak ranging from 300 to 350 nm depending on the change in the local environment.…”
Section: R E T R a C T E Dmentioning
confidence: 98%
“…As widely described, the intrinsic fluorescence emission of tryptophan can be used to probe the changes that occur in the tertiary conformation of oligomeric species formed during the peptide and protein aggregation process. Hence, we compared the fluorescence properties of the tryptophan residues in the PAs with those of the parent peptide in water. As shown in Figure , the emission spectrum of peptide E1P47 in water showed a maximum centered at 356 nm indicating the hydrophilic environment of the W residues.…”
Section: Resultsmentioning
confidence: 99%