Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding-0

<p><b>Copyright information:</b></p><p>Taken from "Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding"</p><p>http://www.biomedcentral.com/1471-2202/8/29</p><p>BMC Neuroscience 2007;8():29-29.</p><p>Published online 2 May 2007</p><p>PMCID:PMC1871596.</p><p></p>rcles) was observed using circular dichroism. (B) Similar β-sheet conformation of TMR-labelled Aβ42 (closed squares) and unlabelled Aβ42 (open squares) was found using circular dichroism. Unstructured conformation of TMR-labelled mutant peptide (closed triangles) is also shown. (C) Thioflavin-T fluorescence indicated similar pH-dependent aggregation profiles for both TMR-labelled Aβ40 (solid line, closed circles) and unlabelled Aβ40 (dashed line, open circles). (D) Thioflavin-T fluorescence also indicated similar aggregation profiles for both TMR-labelled Aβ42 (solid line, closed squares) and unlabelled Aβ42 (dashed line, open squares) as well as very little aggregation produced by the TMR-labelled mutant peptide (dotted line, closed triangles). Electron microscopy images of TMR-labelled Aβ40 and TMR-labelled Aβ42 amyloid fibrils are shown in (E) and (F), respectively, with 100 nm scale bars. The high similarity between labelled and unlabelled peptides suggests that the addition of the fluorescent label has no observable effect on the aggregation profile of Aβ