Hen egg white lysozyme fibrillation: a deep-UV resonance Raman spectroscopic study

被引：62
作者：
Xu, Ming [1 ]
Ermolenkov, Vladimir V. [1 ]
Uversky, Vladimir N. [2 ,3 ]
Lednev, Igor K. [1 ]
机构：
[1] SUNY Albany, Dept Chem, Albany, NY 12222 USA
[2] Indiana Univ, Sch Med, Dept Biochem & Mol Biol, Ctr Computat Biol & Bioinformat, Indianapolis, IN 46202 USA
[3] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia
来源：
JOURNAL OF BIOPHOTONICS | 2008年 / 1卷 / 03期
关键词：
Hen egg white lysozyme; deep-UV resonance Raman spectroscopy; tryptophan fluorescence spectroscopy; circular dichroism spectroscopy; amyloid fibril; fibrillation;
D O I：
10.1002/jbio.200710013
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Amyloid fibrils are associated with numerous degenerative diseases. The molecular mechanism of the structural transformation of native protein to the highly ordered cross-beta structure, the key feature of amyloid fibrils, is under active investigation. Conventional biophysical methods have limited application in addressing the problem because: of the heterogeneous nature of the system, In this study; we demonstrated that deep, UV resonance Raman (DUVRR) Spectroscopy in combination with circular dichroism (CD) and intrinsic tryptophan fluorescence allowed for quantitative characterization of protein structural evolution. at all stages of hen egg white lysozyme fibrillation in vitro. DUVRR spectroscopy was found to lie complimentary to the fur,UV CD because it is (i) more sensitive to beta-sheet than to alpha-helix, and (ii) capable of characterizing quantitatively inhomogeneous and highly light-scattering samples, In addition, phenylalanine, a natural DUVRR spectroscopic biomarker of protein structural rearrangements, exhibited substantial changes in the Raman cross section of the 1000-cm(-1) band at various stages of fibrillation. (C) 2008 by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
引用
收藏
页码：215 / 229
页数：15
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