Distinguishing the cross-beta spine arrangements in amyloid fibrils using FRET analysis.
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.
Deng
Wei
W
Beijing National Laboratory for Molecular Sciences, State Key Laboratory of Structural Chemistry for Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
Cao
Aoneng
A
Lai
Luhua
L
D000682:Amyloid / Q000737:chemistry*; D018360:Crystallography, X-Ray; D031541:Fluorescence Resonance Energy Transfer; D011487:Protein Conformation
D000682:Amyloid