Glycopeptide
(Redirected from Glycopeptides)
Glycopeptide is a type of peptide that contains one or more carbohydrate residues. Glycopeptides are produced by a variety of organisms, including bacteria, fungi, and mammals, and have a wide range of biological activities.
Structure
Glycopeptides are composed of a peptide backbone to which one or more carbohydrate residues are attached. The carbohydrate residues can be simple monosaccharides such as glucose or galactose, or more complex polysaccharides. The peptide backbone can be composed of any combination of the 20 standard amino acids, and the carbohydrate residues can be attached to the peptide backbone at any position.
Biosynthesis
The biosynthesis of glycopeptides involves the action of several enzymes. First, the peptide backbone is synthesized by the ribosome. Then, the carbohydrate residues are attached to the peptide backbone by a process called glycosylation. This process involves the action of enzymes called glycosyltransferases, which transfer the carbohydrate residues from a donor molecule to the peptide backbone.
Biological activity
Glycopeptides have a wide range of biological activities. Some glycopeptides, such as vancomycin and teicoplanin, are used as antibiotics to treat bacterial infections. Other glycopeptides, such as erythropoietin and thyrotropin, are hormones that regulate various physiological processes. Still other glycopeptides, such as mucins, are involved in cell-cell interactions and the immune response.
Clinical significance
Due to their biological activity, glycopeptides have significant clinical significance. Glycopeptide antibiotics are used to treat serious bacterial infections, especially those caused by Gram-positive bacteria. Glycopeptide hormones are used to treat various medical conditions, such as anemia and hypothyroidism. Abnormal glycosylation of glycopeptides can lead to various diseases, such as cancer and autoimmune disorders.
See also
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Contributors: Prab R. Tumpati, MD