Different Dynamics in 6aJL2 Proteins Associated with AL Amyloidosis, a Conformational Disease.

ABSTRACT: Light-chain amyloidosis (AL) is the most common systemic amyloidosis and is caused by the deposition of mainly insoluble immunoglobulin light chain amyloid fibrils in multiple organs, causing organ failure and eventually death. The germ-line λ6a has been implicated in AL, where a single point mutant at amino acid 24 (6aJL2-R24G) has been observed in around 25% of patient samples. Structural analysis has shown only subtle differences between both proteins; nevertheless, 6aJL2-R24G is more prone to form amyloid fibrils. To improve our understanding of the role of protein flexibility in amyloid fibril formation, we have used a combination of solution nuclear magnetic resonance spectroscopy and molecular dynamics simulations to complement the structural insight with dynamic knowledge. Fast tim

SUBMITTER: Maya-Martinez R 

PROVIDER: S-EPMC6747610 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature