Investigating Local Sequence-Structural Attributes of Amyloidogenic Light Chain Variable Domains.

ABSTRACT: Light chain amyloidosis is a medical condition characterized by the aggregation of misfolded antibody light chains into insoluble amyloid fibrils in the target organs, causing organ dysfunction, organ failure, and death. Despite extensive research to understand the factors contributing to amyloidogenesis, accurately predicting whether a given protein will form amyloids under specific conditions remains a formidable challenge. In this study, we have conducted a comprehensive analysis to understand the amyloidogenic tendencies within a dataset containing 1828 (348 amyloidogenic and 1480 non-amyloidogenic) antibody light chain variable region (V_L) sequences obtained from the AL-Base database. Physicochemical and structural features often associated with protein aggregation, such as

SUBMITTER: Rawat P 

PROVIDER: S-EPMC12314586 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature