Morphology-Dependent Interactions between α-Synuclein Monomers and Fibrils.

ABSTRACT: Amyloid fibrils may adopt different morphologies depending on the solution conditions and the protein sequence. Here, we show that two chemically identical but morphologically distinct α-synuclein fibrils can form under identical conditions. This was observed by nuclear magnetic resonance (NMR), circular dichroism (CD), and fluorescence spectroscopy, as well as by cryo-transmission electron microscopy (cryo-TEM). The results show different surface properties of the two morphologies, A and B. NMR measurements show that monomers interact differently with the different fibril surfaces. Only a small part of the N-terminus of the monomer interacts with the fibril surface of morphology A, compared to a larger part of the monomer for morphology B. Differences in ThT binding seen by fluorescence t

SUBMITTER: Palmadottir T 

PROVIDER: S-EPMC10049171 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature