Ontology highlight
ABSTRACT:
SUBMITTER: Marshall KE
PROVIDER: S-EPMC4957119 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Marshall Karen E KE Vadukul Devkee M DM Dahal Liza L Theisen Alina A Fowler Milena W MW Al-Hilaly Youssra Y Ford Lenzie L Kemenes György G Day Iain J IJ Staras Kevin K Serpell Louise C LC
Scientific reports 20160722
Amyloid β1-42 (Aβ1-42) plays a central role in Alzheimer's disease. The link between structure, assembly and neuronal toxicity of this peptide is of major current interest but still poorly defined. Here, we explored this relationship by rationally designing a variant form of Aβ1-42 (vAβ1-42) differing in only two amino acids. Unlike Aβ1-42, we found that the variant does not self-assemble, nor is it toxic to neuronal cells. Moreover, while Aβ1-42 oligomers impact on synaptic function, vAβ1-42 do ...[more]