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Mutant Glycosyltransferases Assist in the Development of a Targeted Drug Delivery System and Contrast Agents for MRI

Overview
Journal AAPS J
Specialty Pharmacology
Date 2006 Apr 6
PMID 16584127
Citations 5
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Abstract

The availability of structural information on glycosyltransferases is beginning to make structure-based reengineering of these enzymes possible. Mutant glycosyltransferases have been generated that can transfer a sugar residue with a chemically reactive unique functional group to a sugar moiety of glycoproteins, glycolipids, and proteoglycans (glycoconjugates). The presence of modified sugar moiety on a glycoprotein makes it possible to link bioactive molecules via modified glycan chains, thereby assisting in the assembly of bionanoparticles that are useful for developing the targeted drug delivery system and contrast agents for magnetic resonance imaging. The reengineered recombinant glycosyltransferases also make it possible to (1) remodel the oligosaccharide chains of glycoprotein drugs, and (2) synthesize oligosaccharides for vaccine development.

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References
1.
Yayon A, Klagsbrun M, Esko J, Leder P, Ornitz D . Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell. 1991; 64(4):841-8. DOI: 10.1016/0092-8674(91)90512-w. View

2.
Couldrey C, Green J . Metastases: the glycan connection. Breast Cancer Res. 2001; 2(5):321-3. PMC: 138652. DOI: 10.1186/bcr75. View

3.
Wright C . Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding. J Biol Chem. 1992; 267(20):14345-52. View

4.
Bourne Y, Bolgiano B, Liao D, Strecker G, Cantau P, Herzberg O . Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nat Struct Biol. 1994; 1(12):863-70. DOI: 10.1038/nsb1294-863. View

5.
Schlessinger J, Lax I, Lemmon M . Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors?. Cell. 1995; 83(3):357-60. DOI: 10.1016/0092-8674(95)90112-4. View