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Glycoconjugate Journal 20, 107118, 2004 C 2004 Kluwer Academic Publishers. Manufactured in The Netherlands.

Summary: Glycoconjugate Journal 20, 107­118, 2004
C 2004 Kluwer Academic Publishers. Manufactured in The Netherlands.
Alpha-Galactosyl trisaccharide epitope:
Modification of the 6-primary positions and
recognition by human anti-Gal antibody
Peter R. Andreana, Przemyslaw Kowal, Adam J. Janczuk and Peng George Wang
Wayne State University, Detroit, MI 48202, USA
Galactose oxidase (EC, GAO) was used to convert the C-6 OH of Gal(1 4)Glc­OBn (5) to the corresponding
hydrated aldehyde (7). Chemical modification, through dehydratative coupling and reductive amination, gave rise to a small
library of Gal(1 4)Glc­OBn analogues (9a­f, 10, 11). UDP-[6-3
H]Gal studies indicated that 1,3-galactosyltransferase
recognized the C-6 modified Gal(1 4)Glc­OBn analogues (9a­f, 10, 11). Preparative scale reactions ensued, utilizing
a single enzyme UDP-Gal conversion as well as a dual enzymatic system (GalE and 1,3GalT), taking full advantage of the
more economical UDP-Glc, giving rise to compounds 6, 15­22. Gal(1 3)Gal(1 4)Glc­OBn trisaccharide (6) was
produced on a large scale (2 g) and subjected to the same chemoenzymatic modification as stated above to produce C-6
modified derivatives (23­30). An ELISA bioassay was performed utilizing human anti-Gal antibodies to study the binding
affinity of the derivatized epitopes (6, 15­30). Modifications made at the C-6 position did not alter the IgG antibody's
ability to recognize the unnatural epitopes. Modifications made at the C-6 position resulted in significant or complete
abrogation of recognition. The results indicate that the C-6 OH of the Gal trisaccharide epitope is not mandatory for
antibody recognition.


Source: Andreana, Peter R. - Department of Chemistry, Wayne State University


Collections: Chemistry