Dissecting Structure of Prion Amyloid Fibrils by Hydrogen鈥揇euterium Exchange Ultraviolet Raman Spectroscopy
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- 作者：Victor Shashilov ; Ming Xu ; Natallia Makarava ; Regina Savtchenko ; Ilia V. Baskakov ; Igor K. Lednev
- 刊名：The Journal of Physical Chemistry B
- 出版年：2012
- 出版时间：July 12, 2012
- 年：2012
- 卷：116
- 期：27
- 页码：7926-7930
- 全文大小：280K
- 年卷期：v.116,no.27(July 12, 2012)
- ISSN：1520-5207
文摘
The molecular mechanisms underlying structural diversity of amyloid fibrils or prion strains formed within the same primary structure is considered to be one of the most enigmatic questions in prion biology. We report here on the direct characterization of amyloid structures using a novel spectroscopic technique, hydrogen鈥揹euterium exchange ultraviolet Raman spectroscopy. This method enables us to assess the structural differences within highly ordered cross-尾-cores of two amyloid states produced within the same amino acid sequence of full-length mammalian prion protein. We found that while both amyloid states consisted of 尾-structures, their cross-尾-cores exhibited hydrogen bonding of different strengths. Moreover, Raman spectroscopy revealed that both amyloid states displayed equally narrow crystalline-like bands, suggesting uniform structures of cross-尾-cores within each state. Taken together, these data suggest that highly polymorphous fibrils can display highly uniform structures of their cross-尾-core and belong to the same prion strain.