Effect of G83R Mutation on Transthyretin Protein Structural Stability.

ABSTRACT: Transthyretin (TTR) G83R mutation can cause vitreous amyloidosis and severely impair vision. Further understanding of the effect of G83R mutation on the TTR structure and stability will help to understand its pathogenesis. This study investigated the thermodynamic and dynamic stabilities, as well as fibril formation, of TTR G83R and compared them with those of wild-type TTR and V30 M variants. Bioinformatics tools (NetSurfP 3.0, DynaMut2, and Desmond) were used to explore the effect of G83R on the TTR protein structural and dynamic stabilities. We explored the effect of G83R on TTR thermodynamic stability using urea-mediated resveratrol and tryptophan fluorescence. The effect of G83R affects TTR aggregation and fibril formation in acidic environments. Molecular dynamics simulation suggeste

SUBMITTER: Chen X 

PROVIDER: S-EPMC12392194 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature