A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.

ABSTRACT: Protein aggregation is linked with the onset of several neurodegenerative disorders, including Parkinson's disease (PD), which is associated with the aggregation of α-synuclein (αSyn). The structural mechanistic details of protein aggregation, including the nature of the earliest protein-protein interactions, remain elusive. In this study, we have used single molecule force spectroscopy (SMFS) to probe the first dimerization events of the central aggregation-prone region of αSyn (residues 71-82) that may initiate aggregation. This region has been shown to be necessary for the aggregation of full length αSyn and is capable of forming amyloid fibrils in isolation. We demonstrate that the interaction of αSyn_71-82 peptides can be studied using SMFS when inserted into a loop of prote

SUBMITTER: Doherty CPA 

PROVIDER: S-EPMC6032367 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature