Abstract
Thioflavin-T is used to image amyloid aggregates because of the excellent turn-on fluorescence properties, but binding affinities are low. By mounting multiple dye units on the surface of a vesicle, the binding affinity for α-synuclein fibrils is increased by three orders of magnitude, and the optical response is increased. Cooperative interactions of the dye headgroup and lipid with the protein provide a general strategy for the construction of multivalent amyloid probes based on vesicles.
Highlights
Thioflavin-T is used to image amyloid aggregates because of the excellent turn-on fluorescence properties, but binding affinities are low
When the DOPC and 1 (DOPC·1) vesicles were added to a solution of sonicated α-synuclein fibrils, the fluorescence intensity increased dramatically in a time dependent manner (Figure 3)
Modest increases in binding affinity have been achieved by synthesizing multivalent ThT derivatives.[10−12] Here we report a supramolecular approach to the assembly of multivalent high contrast probes for protein aggregates
Summary
Thioflavin-T is used to image amyloid aggregates because of the excellent turn-on fluorescence properties, but binding affinities are low. The fluorescence spectrum of the DOPC·1 vesicle solution showed a low intensity emission at
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