Fig. 6
From: N-terminally truncated Aβ4-x proteoforms and their relevance for Alzheimer’s pathophysiology
Biophysical and structural characterization of full-length and truncated Aβ peptides employed in the brain clearance experiments. a Circular Dichroism (CD) analysis to illustrate changes in secondary structure of HIFP-treated peptides freshly solubilized in 10 mM PO4 buffer containing 150 mM NaF (black lines) and the 24-h aggregated counterparts (red lines). In all cases, data represent the mean of 15 scans after subtraction of background readings of the respective buffer blanks. b Fluorescence evaluation of Thioflavin T binding to the respective synthetic homologues either freshly reconstituted (black bars) or after 24-h incubation under physiological salt concentrations (red bars). Results are expressed in arbitrary units (A.U.) and represent the mean ± SEM of three independent experiments after subtraction of blank levels