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Endogenous carbohydrate-binding proteins, commonly known as lectins, are a diverse group of proteins that specifically recognize and bind to complex carbohydrate structures (glycans) on the surface of cells or within the extracellular matrix [1, 2]. These proteins play critical roles in biological processes such as cell-cell adhesion, immune system regulation, and intracellular protein trafficking [3, 13]. In disease states, lectins are often involved in promoting tumor metastasis, chronic inflammation, and the entry of pathogens into host cells [1, 17]. Therapeutic strategies targeting these proteins include the development of glycomimetics and monoclonal antibodies to block pathological interactions, as well as utilizing specific lectins like the asialoglycoprotein receptor for the targeted delivery of RNA-based drugs [3, 8]. Despite their potential, the broad expression and functional redundancy of many lectin families present challenges in achieving high selectivity and avoiding off-target effects [8, 13].
Inhibition of carbohydrate-mediated cell adhesion and signaling; targeted delivery of therapeutics via receptor-mediated endocytosis.
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