Site-Specific Immobilization Boosts the Performance of a Galectin-1 Biosensor.

ABSTRACT: The analysis of protein-bound glycans has gained significant attention due to their pivotal roles in physiological and pathological processes like cell-cell recognition, immune response, and disease progression. Routine methods for glycan analysis are challenged by the very similar physicochemical properties of their carbohydrate components. As an alternative, lectins, which are proteins that specifically bind to glycans, have been integrated into biosensors for glycan detection. However, the effectiveness of protein-based biosensors depends heavily on the immobilization of proteins on the sensor surface. To enhance the sensitivity and/or selectivity of lectin biosensors, it is crucial to immobilize the lectin in an optimal orientation for ligand binding without compromising its function.

SUBMITTER: Kolanovic D 

PROVIDER: S-EPMC11660155 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature