Distinguishing the cross-beta spine arrangements in amyloid fibrils using FRET analysis.

Protein Science : a Publication of the Protein Society
Wei DengLuhua Lai

Abstract

The recently published microcrystal structures of amyloid fibrils from small peptides greatly enhanced our understanding of the atomic-level structure of the amyloid fibril. However, only a few amyloid fibrils can form microcrystals. The dansyl-tryptophan fluorescence resonance energy transfer (FRET) pair was shown to be able to detect the inter-peptide arrangement of the Transthyretin (105-115) amyloid fibril. In this study, we combined the known microcrystal structures with the corresponding FRET efficiencies to build a model for amyloid fibril structure classification. We found that fibrils with an antiparallel structural arrangement gave the largest FRET signal, those with a parallel arrangement gave the lowest FRET signal, and those with a mixed arrangement gave a moderate FRET signal. This confirms that the amyloid fibril structure patterns can be classified based on the FRET efficiency.

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Citations

May 5, 2011·Biophysical Journal·Joshua T BerrymanSarah A Harris
Apr 22, 2010·Journal of the American Chemical Society·Ludmila A PopovaIgor K Lednev
Nov 22, 2011·Biochemical and Biophysical Research Communications·Dong XiLuhua Lai
Nov 30, 2016·Chembiochem : a European Journal of Chemical Biology·Heng Chi, Timothy A Keiderling
Jan 7, 2021·Chembiochem : a European Journal of Chemical Biology·Suvrat ChowdharyBeate Koksch
Dec 14, 2017·Journal of the American Chemical Society·Waldemar HoffmannKevin Pagel

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