Mutant glycosyltransferases assist in the development of a targeted drug delivery system and contrast agents for MRI.
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.
Qasba
Pradman K
PK
Structural Glycobiology Section, Nanobiology Program, CCR, NCI-Frederick, Frederick, MD, USA. qasba@helix.nih.gov
Ramakrishnan
Boopathy
B
Boeggeman
Elizabeth
E
D000818:Animals; D003287:Contrast Media / Q000138:chemical synthesis*; D016503:Drug Delivery Systems / Q000379:methods*; D005818:Genetic Engineering / Q000379:methods; D006001:Glycoconjugates / Q000737:chemistry* / Q000235:genetics*; D016695:Glycosyltransferases / Q000138:chemical synthesis* / Q000235:genetics*; D006801:Humans; D008279:Magnetic Resonance Imaging / Q000379:methods*
D003287:Contrast Media; D006001:Glycoconjugates; D016695:Glycosyltransferases