Fig. 8
From: In vivo induction of membrane damage by β-amyloid peptide oligomers
Biarsenical dye staining of dicysteine-tagged synthetic wild type and Gly37Leu variant Aβ1–42 in cultured hippocampal neurons. a Schematic model of how membrane-associated Aβ dimers in a parallel α-helical arrangement could bind the biarsenical FlAsH reagent. b Super-resolution image of cultured hippocampal neurons exposed to synthetic wild type Aβ1–42, treated with FlAsH reagent, fixed, permeabilized, and probed with anti-Aβ antibody 6E10. Note minimal association of FlAsH signal with Aβ immunoreactivity, expected because this synthetic peptide does not contain dicysteines. c Same experiment as described for panel “B”, except treatment with synthetic dicysteine-tagged wild type Aβ. Note multiple foci of co-localized FlAsH and Aβ staining (arrows). d Same experiment as described for panel “B”, except treatment with synthetic dicysteine-tagged Gly37Leu Aβ. Note this substitution prevents the formation of co-staining foci, supporting the hypothesis that the Gly37Leu substitution inhibits the assembly of (potentially pore-forming) multimers. (The increased neuronal process-associated FlAsH signal in the Gly37Leu Aβ -treated cultures may reflect increased non-specific uptake of the FlAsH dye, because neurons treated with the non-toxic Gly37Leu Aβ are healthier than neurons treated with wild type Aβ peptides.) e Quantification of co-labeling foci from multiple image fields acquired in the experiments described in b-d