Alpha1–2-Fucosyltransferase for Enzymatic Synthesis of Alpha1–2-linked Fucosylated Glycans
Excellent yields with defined regio- and stereoselectivity Simplified isolation and purification Faster and more efficient than chemical synthetic methods Reactions can be carried out in aqueous solutions Avoids toxic solvents
Potential target for therapeutic development for treating cancer, bacterial and viral infection, and inflammation Synthesis of important fucosides that play a protective role in human milk for nursing infants
Alpha1–2-linked fucosides are important for their potential application in treating inflammation, bacterial and viral infection and cancer. They are also major components of human milk oligosaccharides. Therefore, they are desirable synthetic targets for therapeutic and prebiotic development. The acid lability, however, make the chemical construction of the fucosidic bond difficult. Fucosyltransferase-catalyzed methods that are highly efficient and selective can be an indispensable resource in obtaining biomedically important fucoside-containing glycans and other biomolecules. Researchers at the University of California, Davis have discovered an alpha1–2-fucosyltransferase that efficiently catalyzes the synthesis of alpha1–2-linked fucosylated glycans containing different internal glycans. With a one-pot multienzyme startegy, Te1-2FT-catalyzed fucosylation reactions were accomplished without needing high-cost sugar nucleotides or isolation of intermediates. Synthesis typically occurs in less than 24 hours, and purification and characterization of the product can be completed in less than 3 days, making this process faster and more efficient than chemical synthetic approaches. Finally, the enzyme reactions can be carried out in aqueous solutions, avoiding toxic organic solvents.
Additional Technologies by these Inventors Tech ID/UC Case 27432/2015-838-0 Related Cases 2015-838-0
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