Resolving the nanoscale structure of β-sheet assemblies using single-molecule orientation-localization microscopy.

ABSTRACT: Synthetic peptides that self-assemble into cross-β fibrils have remarkable utility as engineered biomaterials due to their modularity and biocompatibility, but their structural and morphological similarity to amyloid species has been a long-standing concern for their translation. Further, their polymorphs are difficult to characterize using spectroscopic and imaging techniques that rely on ensemble averaging to achieve high resolution. Here, we utilize single-molecule orientation-localization microscopy (SMOLM) to characterize fibrils formed by the designed amphipathic enantiomers, KFE8^L and KFE8^D, and the pathological amyloid-beta peptide Aβ42. SMOLM reveals that the orientations of Nile red, as it transiently binds to both KFE8 and Aβ42, are consistent with a helica

SUBMITTER: Zhou W 

PROVIDER: S-EPMC10515885 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature