Spectroscopic analysis of metal ions effect on the aggregation of a lambda 6aJL2R24G protein variant

Light-chain amyloidosis (AL) is one of the most common forms of amyloidosis. It is characterized by the extracellular deposition of variable domain fragments of immunoglobulin light chains. The clinical manifestations of this disease vary because the deposits can be found in almost all the organs of the human body causing various failures. Approximately 30% of AL cases contain a λ6a germline and 25% of those cases presents a Glycine at position 24 instead of Arginine (R24G). This mutation causes the protein to be thermodynamically more unstable and to be more amyloidogenic.