Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

0377487 - MBÚ 2013 RIV DE eng J - Článek v odborném periodiku
Kupper, E. Ch. - Rosencrantz, R. R. - Henßen, B. - Pelantová, Helena - Thönes, S. - Drozdová, Anna - Křen, Vladimír - Elling, L.
Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment.
Beilstein Journal of Organic Chemistry. Roč. 8, MAY 9 2012 (2012), s. 712-725. ISSN 1860-5397. E-ISSN 1860-5397
Grant CEP: GA MŠMT OC09045
Klíčová slova: chemo-enzymatic synthesis * galactose oxidase * glycosyltransferase
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.801, rok: 2012

The importance of glycans in biological systems is highlighted by their various functions in physiological and pathological processes. Many glycan epitopes on glycoproteins and glycolipids are based on N-acetyllactosamine units (LacNAc; Gal beta 1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Gal beta 1,4GlcNAc](n)). Poly-LacNAc itself has been identified as a binding motif of galectins, an important class of lectins with functions in immune response and tumorigenesis. Therefore, the synthesis of natural and modified poly-LacNAc glycans is of specific interest for binding studies with galectins as well as for studies of their possible therapeutic applications. We present the oxidation by galactose oxidase and subsequent chemical or enzymatic modification of terminal galactose and N-acetylgalactosamine residues of poly-N-acetyllactosamine (poly-LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) by galactose oxidase
Trvalý link: http://hdl.handle.net/11104/0209632