Dissecting the Structural Organization of Multiprotein Amyloid Aggregates Using a Bottom-Up Approach.

ABSTRACT: Deposition of fibrillar amyloid β (Aβ) in senile plaques is a pathological signature of Alzheimer's disease. However, senile plaques also contain many other components, including a range of different proteins. Although the composition of the plaques can be analyzed in post-mortem tissue, knowledge of the molecular details of these multiprotein inclusions and their assembly processes is limited, which impedes the progress in deciphering the biochemical mechanisms associated with Aβ pathology. We describe here a bottom-up approach to monitor how proteins from human cerebrospinal fluid associate with Aβ amyloid fibrils to form plaque particles. The method combines flow cytometry and mass spectrometry proteomics and allowed us to identify and quantify 128 components of the captured multiprotei

SUBMITTER: Chaudhary H 

PROVIDER: S-EPMC7243255 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature