A kinetic coupling between protein unfolding and aggregation controls time-dependent solubility of the human myeloma antibody light chain.

ABSTRACT: Protein aggregation is one of the most critical processes affecting protein solubility in various contexts-from protein therapeutics formulation to protein diseases. In general, time-dependent changes in protein solubility are complex kinetically driven processes that often involve a triggering event that consists of a protein unfolding/misfolding followed by the assembling of aggregation-competent protein species. In this study, we have examined the relation between stability and time-dependent solubility of the recombinant human antibody light chain, hLC, which was found to form renal tubular casts in the multiple myeloma patient. To analyze the aggregation quantitatively, the hLC stability and protein solubility assays were performed in vitro at elevated temperatures. A differential acc

SUBMITTER: Dzupponova V 

PROVIDER: S-EPMC7679964 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature