Demystifying multipronged approaches of wheat germ agglutinin-mediated drug delivery, targeting, and imaging: An explicative review

Wheat germ agglutinin (WGA) is a heterodimer lectin having a molecular weight of 38 kDa. It is found in wheat grains that can bind to specific carbohydrate moieties on cell surfaces, produced by Triticum vulgare. WGA exhibits a considerable affinity for specific sugar residues that are commonly present on intracellular and cell-surface glycoproteins and glycolipids, such as sialic acid (N-acetylneuraminic acid) and N-acetyl glucosamine (GlcNAc). Sialic acids are terminal sugars found on cell surface glycoconjugates, acting as ligands for cell surface receptors like Siglecs. They are essential for cellular recognition, cell-cell attachment, and signaling. On the other hand, N-acetylglucosamine is a component of complex carbohydrates and is involved in various cellular processes. In the presence of WGA, sialic acids on glycoproteins can mask Siglecs, preventing their binding to external pathogens. This interaction highlights the significance of sialic acid and N-acetylglucosamine in modulating cell surface interactions and immune responses, demonstrating their importance in biological processes. Applications include labeling glycoproteins in cells, identifying aberrant glycosylation patterns, and evaluating. WGA is useful in biomedical research because of its unique qualities and range of uses. It is particularly beneficial because of its ability to bind specifically to N-acetylglucosamine residues on glycoproteins, making it a useful tool for studying cell surface interactions, cellular recognition, and signaling pathways. Additionally, WGA has been utilized in various biomedical applications such as targeted drug delivery, imaging, biomarkers, and cancer cell death induction, among others, which have created an impact on advanced treatment approaches. [Display omitted]