Glycosidic linkage

A glycosidic linkage is a type of covalent bond that joins a carbohydrate molecule to another group, which may or may not be another carbohydrate (NCBI, 2023). These linkages are formed through a condensation reaction between the hemiacetal or hemiketal group of a saccharide and the hydroxyl group of another compound (IUPAC Gold Book, 2014). They are essential for the synthesis of complex polysaccharides like starch and cellulose, as well as the glycosylation of proteins and lipids (Alberts et al., 2014). In biological systems, these bonds facilitate energy storage, provide structural support, and enable cell-cell recognition (Molecular Biology of the Cell, 2014). While the linkage itself is a chemical bond rather than a protein or receptor, the enzymes that create or break these bonds are significant therapeutic targets (StatPearls, 2023). For example, alpha-glucosidase inhibitors like acarbose target the enzymes that hydrolyze these bonds in the digestive tract to manage blood glucose in type 2 diabetes (PubMed, 2022). Similarly, neuraminidase inhibitors like oseltamivir prevent the cleavage of glycosidic linkages on sialic acid, which is necessary for the release of influenza virus particles (PubChem, 2024). Genetic defects in the enzymes responsible for degrading specific glycosidic linkages result in lysosomal storage diseases, such as Gaucher's or Fabry disease (NIH, 2023). Consequently, therapeutic strategies often focus on modulating the activity of these enzymes to treat metabolic, infectious, and genetic disorders (Nature Reviews Drug Discovery, 2021).

Other names

Glycosidic bondO-glycosidic bondN-glycosidic bondS-glycosidic bondC-glycosidic bond

Inhibition or replacement of enzymes (glycosidases or glycosyltransferases) that catalyze the hydrolysis or formation of glycosidic bonds.