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- W2912678015 abstract "A fluorescent bis-styryl-benzothiadiazole (BTD) with carboxylic acid functional groups (X-34/Congo red analogue) showed lower binding affinity toward Aβ1-42 and Aβ1-40 fibrils than its neutral analogue. Hence, variable patterns of neutral OH-substituted bis-styryl-BTDs were generated. All bis-styryl-BTDs showed higher binding affinity to Aβ1-42 fibrils than to Aβ1-40 fibrils. The para-OH on the phenyl rings was beneficial for binding affinity while a meta-OH decreased the affinity. Differential staining of transgenic mouse Aβ amyloid plaque cores compared to peripheral coronas using neutral compared to anionic bis-styryl ligands indicate differential recognition of amyloid polymorphs. Hyperspectral imaging of transgenic mouse Aβ plaque stained with uncharged para-hydroxyl substituted bis-styryl-BTD implicated differences in binding site polarity of polymorphic amyloid plaque. Most properties of the corresponding bis-styryl-BTD were retained with a rigid alkyne linker rendering a probe insensitive to cis–trans isomerization. These new BTD-based ligands are promising probes for spectral imaging of different Aβ fibril polymorphs." @default.
- W2912678015 created "2019-02-21" @default.
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- W2912678015 date "2019-02-01" @default.
- W2912678015 modified "2023-09-25" @default.
- W2912678015 title "Phenolic Bis-styrylbenzo[<i>c</i>]-1,2,5-thiadiazoles as Probes for Fluorescence Microscopy Mapping of Aβ Plaque Heterogeneity" @default.
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- W2912678015 doi "https://doi.org/10.1021/acs.jmedchem.8b01681" @default.
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