Comparative study of the stabilities of synthetic in vitro and natural ex vivo transthyretin amyloid fibrils.

ABSTRACT: Systemic amyloidosis caused by extracellular deposition of insoluble fibrils derived from the pathological aggregation of circulating proteins, such as transthyretin, is a severe and usually fatal condition. Elucidation of the molecular pathogenic mechanism of the disease and discovery of effective therapies still represents a challenging medical issue. The in vitro preparation of amyloid fibrils that exhibit structural and biochemical properties closely similar to those of natural fibrils is central to improving our understanding of the biophysical basis of amyloid formation in vivo and may offer an important tool for drug discovery. Here, we compared the morphology and thermodynamic stability of natural transthyretin fibrils with those of fibrils generated in vitro e

SUBMITTER: Raimondi S 

PROVIDER: S-EPMC7450123 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature