Article
RNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis.
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis - 1 Sept 2026
Naser Eyad, Oubari Sara, Jakob Josefine, Häupl Björn, Budeus Bettina, Walkenfort Bernd, Nowakowski Melanie, Hessler Gabriele, Kühn Claudine, Hasenberg Mike, Oellerich Thomas, Reinhardt Hans Christian, Carpinteiro Alexander
Abstract excerpt
BACKGROUND: Systemic light chain amyloidosis is a protein misfolding disorder characterized by deposition of clonal immunoglobulin light chains in vital organs. To date, little is known about the contribution of light chain constant domain mutations in thermodynamic stability and amyloidogenicity. METHODS: In 89 patients, RNA-based full-length light chain repertoire sequencing with Oxford Nanopore was performed,...
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- Humans
- Mutation
- Thermodynamics
- Molecular Dynamics Simulation