Hen Egg White Lysozyme Fibrillation: a Deep-uv Resonance Raman Spectroscopic Study
Document Type
Article
Publication Date
2008
Digital Object Identifier (DOI)
https://doi.org/10.1002/jbio.200710013
Abstract
Amyloid fibrils are associated with numerous degenerative diseases. The molecular mechanism of the structural transformation of native protein to the highly ordered cross-β 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 be complimentary to the far-UV CD because it is (i) more sensitive to β -sheet than to α -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. (© 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Biophotonics, v. 1, issue 3, p. 215-229
Scholar Commons Citation
Xu, Ming; Ermolenkov, Vladimir V.; Uversky, Vladimir N.; and Lednev, Igor K., "Hen Egg White Lysozyme Fibrillation: a Deep-uv Resonance Raman Spectroscopic Study" (2008). Molecular Medicine Faculty Publications. 798.
https://digitalcommons.usf.edu/mme_facpub/798
