Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.

ABSTRACT: Amyloid oligomers are considered the most neurotoxic species of amyloid aggregates. Spontaneous assembly of amyloids into aggregates is recognized as a major molecular mechanism behind Alzheimer's disease and other neurodegenerative disorders involving protein aggregation. Characterization of such oligomers is extremely challenging but complicated by their transient nature. Previously, we introduced a flexible nanoarray (FNA) method enabling us to probe dimers assembled by the amyloid β (14-23) [Aβ (14-23)] peptide. The study presented herein modifies and enhances this approach to assemble and probe trimers of Aβ (14-23). A metal-free click chemistry approach was used, in which dibenzocyclooctyne (DBCO) groups were incorporated at selected sites within the FNA template to click Aβ (14-23)

SUBMITTER: Maity S 

PROVIDER: S-EPMC6093788 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature