ArticleBioconjugate chemistry2024
Site-Specific Immobilization Boosts the Performance of a Galectin-1 Biosensor.
Article in Bioconjugate chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.ACS omega · 2026Article
- Beyond Self-Assembly: Bioorthogonal 'Click' Chemistry Strategies for Robust Electrochemical Interfaces in Wearable Biosensors.Biosensors · 2026Review
- Biodetection of Mycobacterium tuberculosis: nano-biosensors in detection; from principles to recent progresses.Journal of biological engineering · 2026Review
- The role of glycan-lectin interactions in the tumor microenvironment: immunosuppression regulators of colorectal cancer.American journal of cancer research · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
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. Random immobilization methods often result in arbitrary orientation and reduced sensitivity. To address this, we explored a directed immobilization strategy relying on a reactive noncanonical amino acid (ncAA) and bioorthogonal chemistry. In this study, we site-specifically incorporated the reactive noncanonical lysine derivative, N
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