Computational Analysis of the Interactions between the S100B Extracellular Chaperone and Its Amyloid β Peptide Client.

ABSTRACT: S100B is an astrocytic extracellular Ca²⁺-binding protein implicated in Alzheimer's disease, whose role as a holdase-type chaperone delaying Aβ₄₂ aggregation and toxicity was recently uncovered. Here, we employ computational biology approaches to dissect the structural details and dynamics of the interaction between S100B and Aβ₄₂. Driven by previous structural data, we used the Aβ_25-35 segment, which recapitulates key aspects of S100B activity, as a starting guide for the analysis. We used Haddock to establish a preferred binding mode, which was studied with the full length Aβ using long (1 μs) molecular dynamics (MD) simulations to investigate the structural dynamics and obtain representative interaction complexes. From the analysis, Aβ-Lys28 e

SUBMITTER: Rodrigues FEP 

PROVIDER: S-EPMC8037576 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature