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Fluorescence and phosphorescence of tryptophan in peptides of different length and sequence

Paper ID Volume ID Publish Year Pages File Format Full-Text
29377 44372 2016 9 PDF Available
Title
Fluorescence and phosphorescence of tryptophan in peptides of different length and sequence
Abstract

•All peptides and Trp show double exponential decay of fluorescence and luminescence.•Both short and long fluorescence lifetimes increase with peptide length.•Peptides' luminescence spectrum contains a structured and a non-structured component.•Unstructured and structured spectrum decay with short and long lifetime respectively.•Amplitudes of long fluorescence lifetime and short luminescence lifetime are similar.

To interpret accurately protein fluorescence and phosphorescence, it is essential to achieve a better understanding of the luminescence properties of tryptophan (Trp, or W) in peptides. In published literature data on luminescence of peptides of varied length are scarce. This article describes studies of fluorescence and phosphorescence properties of the eight Trp-containing synthetic peptides: WAK, AWK, SWA, KYLWE, AVSWK, WVSWAK, WAKLAWE, and AVSWAKLARE. The aim was to investigate which factors influence the fluorescence yield and phosphorescence-spectra and lifetimes. Absorption spectra, room temperature fluorescence emission and corresponding excitation spectra and time-resolved phosphorescence spectra (77 K) have been recorded; the dependence of the fluorescence quantum yield on the specific peptide and its variation with the wavelength of excitation has been studied. The changes in fluorescence yield and shape of phosphorescence spectra are explained in terms of internal electron and proton transfer. The structured phosphorescence spectrum originates from proton transfer occurring upon excitation of Trp, while electron transfer gives rise to a non-structured luminescence spectrum. There is also electron transfer from higher vibronic S1 states. In the peptides there is higher probability of electron transfer than in Trp alone. The obtained data are interpreted in light of the peptides' sequence, length and conformation.

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Keywords
Luminescence; Peptides; Phosphorescence; Steady state fluorescence; Time resolved fluorescence; Tryptophan
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Fluorescence and phosphorescence of tryptophan in peptides of different length and sequence
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 157, April 2016, Pages 120–128
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us