Frutalin as an Affinity Tool for sIgA1: Biophysical and Structural Characterization of the Lectin-Antibody Complex.

ABSTRACT: Secretory immunoglobulin A1 (sIgA1) is the predominant antibody in mucosal secretions and human colostrum, where it plays critical roles in immune exclusion and microbiota regulation. Due to its high degree of glycosylation, oligomeric variability, and structural flexibility, selective purification of sIgA1 remains a technical challengeyet essential for biomedical, immunological, and biotechnological applications, including diagnostic platforms and passive immunotherapy. In this study, frutalin (FTL), a galactose-specific lectin from Artocarpus incisa, was used as both a selective ligand and a structural probe to investigate its interaction with native sIgA1. FTL was immobilized on CNBr-activated agarose to generate an affinity matrix (frutalin-agarose), enabling the efficient puri

SUBMITTER: Costa RCC 

PROVIDER: S-EPMC12713436 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature