Universität zu Köln

Rech, Claudia, Rosencrantz, Ruben R., Krenek, Karel, Pelantova, Helena ORCID: 0000-0002-2523-7413, Bojarova, Pavla ORCID: 0000-0001-7069-0973, Roemer, Christiane E., Hanisch, Franz-Georg, Kren, Vladimir and Elling, Lothar ORCID: 0000-0002-3654-0397 (2011). Combinatorial One-Pot Synthesis of Poly-N-acetyllactosamine Oligosaccharides with Leloir-Glycosyltransferases. Adv. Synth. Catal., 353 (13). S. 2492 - 2501. WEINHEIM: WILEY-V C H VERLAG GMBH. ISSN 1615-4169

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Abstract

Poly-N-acetyllactosamine (Poly-LacNAc, [3Gal beta 1,4GlcNAc beta 1](n)) glycans play an essential role in carbohydrate-protein interactions. The synthesis of poly-LacNAc, both chemical and enzymatic, is typically characterized by high losses of product during sequential synthesis, due to deprotection and/or purification steps. In this work we present a one-pot synthesis of poly-LacNAc oligosaccharides by combining recombinant glycosyltransferases. By fractionation of the poly-LacNAc glycan mixture we were able to isolate glycans with up to six N-acetyllactosamine (LacNAc) units. Activity measurements of the involved recombinant beta 1,4-galactosyltransferase-1 (beta 4GalT-1) and beta 1,3-N-acetylglucosaminyltransferase (beta 3GlcNAcT) with isolated glycan substrates of up to eight sugar units revealed a preference of beta 3GlcNAcT for the tetrasaccharide and no preference of beta 4GalT-1 for a specific glycan length. These findings led us to the optimization of combinatorial one-pot synthesis by variation of substrate and enzyme ratios, as well as starting the synthesis with various poly-LacNAc chain lengths. Consequently, we present here an optimized poly-LacNAc synthesis by the combination of two glycosyltransferases and a uridine-diphospho-glucose/N-acetylglucosamine 4'-epimerase as one-pot strategy resulting in long poly-LacNAc glycans with up to six LacNAc units in high yields while minimizing reaction time and product loss. The obtained products are important ligands for the biofunctionalization of biomaterial surfaces and the construction of an artificial extracellular matrix for tissue engineering.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Rech, Claudia UNSPECIFIED UNSPECIFIED UNSPECIFIED Rosencrantz, Ruben R. UNSPECIFIED UNSPECIFIED UNSPECIFIED Krenek, Karel UNSPECIFIED UNSPECIFIED UNSPECIFIED Pelantova, Helena UNSPECIFIED orcid.org/0000-0002-2523-7413 UNSPECIFIED Bojarova, Pavla UNSPECIFIED orcid.org/0000-0001-7069-0973 UNSPECIFIED Roemer, Christiane E. UNSPECIFIED UNSPECIFIED UNSPECIFIED Hanisch, Franz-Georg UNSPECIFIED UNSPECIFIED UNSPECIFIED Kren, Vladimir UNSPECIFIED UNSPECIFIED UNSPECIFIED Elling, Lothar UNSPECIFIED orcid.org/0000-0002-3654-0397 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-490110
DOI:	10.1002/adsc.201100375
Journal or Publication Title:	Adv. Synth. Catal.
Volume:	353
Number:	13
Page Range:	S. 2492 - 2501
Date:	2011
Publisher:	WILEY-V C H VERLAG GMBH
Place of Publication:	WEINHEIM
ISSN:	1615-4169
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language I-EXTENSION ENZYME; CHEMOENZYMATIC SYNTHESIS; ESCHERICHIA-COLI; BLOOD-GROUP; LINKED OLIGOSACCHARIDES; ERYTHROCYTE-MEMBRANE; RECOMBINANT PROTEIN; CELL-ADHESION; HEAT-SHOCK; GALECTINS Multiple languages Chemistry, Applied; Chemistry, Organic Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/49011