Lectin Affinity Chromatography: Advances in Purification Matrices, Ligand Design, Biomedical Applications, and Scale-Up
TL;DR
This review focuses on the purification of lectins using affinity chromatography, highlighting commonly used matrices, ligands, and elution strategies and its limitations, including cost and operational complexity.
Abstract
Lectins are carbohydrate-binding proteins present in nature in various plant and animal sources. Lectins have been shown to play vital roles in immunological responses, identification of pathogens, and applications in medical therapies like cancer treatment and antiviral drugs. Purity of lectins is crucial for biological activity, hence the need for efficient methods of isolation. One of the most effective ways of purifying lectins is by means of affinity chromatography, because of the reversible lectin-carbohydrate binding mechanism. This review focuses on the purification of lectins using affinity chromatography, highlighting commonly used matrices, ligands, and elution strategies. The advantages of this method, such as high purity, selectivity, and preservation of biological activity, are discussed alongside its limitations, including cost and operational complexity. Recent advancements in matrix development and ligand design are also briefly addressed. Looking ahead, researchers are developing cheaper, reusable materials and automated systems to make lectin purification faster and more scalable. Affinity chromatography remains the undisputed gold standard for lectin purification, and new innovations will expand its impact in medicine and biotechnology.