Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients.

ABSTRACT: Increasing evidence supports the hypothesis that soluble misfolded protein assemblies contribute to the degeneration of postmitotic tissue in amyloid diseases. However, there is a dearth of reliable nonantibody-based probes for selectively detecting oligomeric aggregate structures circulating in plasma or deposited in tissues, making it difficult to scrutinize this hypothesis in patients. Hence, understanding the structure-proteotoxicity relationships driving amyloid diseases remains challenging, hampering the development of early diagnostic and novel treatment strategies. We report peptide-based probes that selectively label misfolded transthyretin (TTR) oligomers circulating in the plasma of TTR hereditary amyloidosis patients exhibiting a predominant neuropathic phenotype. These probes

SUBMITTER: Schonhoft JD 

PROVIDER: S-EPMC5628019 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature