Exploring the sequence features determining amyloidosis in human antibody light chains.

ABSTRACT: The light chain (AL) amyloidosis is caused by the aggregation of light chain of antibodies into amyloid fibrils. There are plenty of computational resources available for the prediction of short aggregation-prone regions within proteins. However, it is still a challenging task to predict the amyloidogenic nature of the whole protein using sequence/structure information. In the case of antibody light chains, common architecture and known binding sites can provide vital information for the prediction of amyloidogenicity at physiological conditions. Here, in this work, we have compared classical sequence-based, aggregation-related features (such as hydrophobicity, presence of gatekeeper residues, disorderness, β-propensity, etc.) calculated for the CDR, FR or V_L regions of amyloido

SUBMITTER: Rawat P 

PROVIDER: S-EPMC8253744 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature