Metal interactions of α-synuclein probed by NMR amide-proton exchange.

ABSTRACT: The aberrant aggregation of α-synuclein (αS), a disordered protein primarily expressed in neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's disease. It is now established that αS has a weak affinity for metal ions and that these interactions alter its conformational properties by generally promoting self-assembly into amyloids. Here, we characterised the nature of the conformational changes associated with metal binding by αS using nuclear magnetic resonance (NMR) to measure the exchange of the backbone amide protons at a residue specific resolution. We complemented these experiments with ¹⁵N relaxation and chemical shift perturbations to obtain a comprehensive map of the interaction between αS and divalent (Ca²⁺, Cu²⁺, Mn

SUBMITTER: Gonzalez-Garcia M 

PROVIDER: S-EPMC10187754 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature