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Effect of fibrillation on the excited state dynamics of tryptophan in serum protein – A time-resolved fluorescence study

Paper ID Volume ID Publish Year Pages File Format Full-Text
26396 43950 2015 7 PDF Available
Title
Effect of fibrillation on the excited state dynamics of tryptophan in serum protein – A time-resolved fluorescence study
Abstract

•Understanding the water relaxation dynamics in HSA amyloid fibril.•Despite having more ordered structure, tryptophan in fibril experiences more labile water.•Microheterogeneity in the protein increases on fibrillation.

The aggregation of proteins into the amyloid fibrils is mainly responsible for several neurological diseases. Knowledge of dynamics in amyloid fibril is very essential to understand its biological activity. Although, the effects of environment like pH, ionic strength, temperature, etc. on the fibril have been studied extensively, studies on the dynamics of amyloid fibril and the role of water in fibril are scarce. In this article, we have reported the results on the excited state dynamics of amyloid fibrils formed by a well-known blood plasma protein, human serum albumin (HSA), at neutral pH. The sole tryptophan residue, W214, has been used as the intrinsic fluorescent probe to monitor its excited state dynamics. Steady-state and time-resolved fluorescence data suggests that the W214 becomes more closer to the quencher amino acid residues in the fibrillar phase than in the native protein. From detailed time-resolved emission measurements, it is shown that despite having a more ordered structure, the water molecules around W214 in amyloid fibril is more labile than that in the native protein. Fluorescence depolarization studies also indicate that the W214 residue is located in a relatively more flexible region of the ordered amyloid fibril than that in the native protein.

Graphical abstractSolvent relaxation dynamics in amyloid fibril.Figure optionsDownload full-size imageDownload as PowerPoint slide

Keywords
Amyloid fibril; Time-resolved fluorescence; Solvation dynamics; Human serum albumin
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Effect of fibrillation on the excited state dynamics of tryptophan in serum protein – A time-resolved fluorescence study
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 299, 15 February 2015, Pages 73–79
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