Liposome Enhanced Detection of Amyloid Protein Aggregates | Zendy

István Kocsis | Zendy; Elena Sanna | Zendy; Christopher A. Hunter | Zendy

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Liposome Enhanced Detection of Amyloid Protein Aggregates

Author(s) -

István Kocsis,

Elena Sanna,

Christopher A. Hunter

Publication year - 2021

Publication title -

organic letters

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/acs.orglett.0c03597

Subject(s) - chemistry , thioflavin , liposome , vesicle , biophysics , fluorescence , amyloid (mycology) , binding affinities , protein aggregation , fibril , affinities , lipid vesicle , amyloid fibril , biochemistry , amyloid β , membrane , alzheimer's disease , receptor , medicine , inorganic chemistry , physics , disease , pathology , quantum mechanics , biology

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.

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