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

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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycan...
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Gespeichert in:

Autor*in:	Christiane E. Kupper [verfasserIn] Ruben R. Rosencrantz [verfasserIn] Birgit Henßen [verfasserIn] Helena Pelantová [verfasserIn] Stephan Thönes [verfasserIn] Anna Drozdová [verfasserIn] Vladimir Křen [verfasserIn] Lothar Elling [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2012

Schlagwörter:	chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine

Übergeordnetes Werk:	In: Beilstein Journal of Organic Chemistry - Beilstein-Institut, 2005, 8(2012), 1, Seite 712-725
Übergeordnetes Werk:	volume:8 ; year:2012 ; number:1 ; pages:712-725

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3762/bjoc.8.80

Katalog-ID:	DOAJ004208951

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520			\|a 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications.
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allfields	10.3762/bjoc.8.80 doi (DE-627)DOAJ004208951 (DE-599)DOAJ14da70ba5b8e42869e3c50896eb2091b DE-627 ger DE-627 rakwb eng QD241-441 Christiane E. Kupper verfasserin aut Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry Ruben R. Rosencrantz verfasserin aut Birgit Henßen verfasserin aut Helena Pelantová verfasserin aut Stephan Thönes verfasserin aut Anna Drozdová verfasserin aut Vladimir Křen verfasserin aut Lothar Elling verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 712-725 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:712-725 https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b kostenfrei https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 712-725
spelling	10.3762/bjoc.8.80 doi (DE-627)DOAJ004208951 (DE-599)DOAJ14da70ba5b8e42869e3c50896eb2091b DE-627 ger DE-627 rakwb eng QD241-441 Christiane E. Kupper verfasserin aut Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry Ruben R. Rosencrantz verfasserin aut Birgit Henßen verfasserin aut Helena Pelantová verfasserin aut Stephan Thönes verfasserin aut Anna Drozdová verfasserin aut Vladimir Křen verfasserin aut Lothar Elling verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 712-725 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:712-725 https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b kostenfrei https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 712-725
allfields_unstemmed	10.3762/bjoc.8.80 doi (DE-627)DOAJ004208951 (DE-599)DOAJ14da70ba5b8e42869e3c50896eb2091b DE-627 ger DE-627 rakwb eng QD241-441 Christiane E. Kupper verfasserin aut Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry Ruben R. Rosencrantz verfasserin aut Birgit Henßen verfasserin aut Helena Pelantová verfasserin aut Stephan Thönes verfasserin aut Anna Drozdová verfasserin aut Vladimir Křen verfasserin aut Lothar Elling verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 712-725 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:712-725 https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b kostenfrei https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 712-725
allfieldsGer	10.3762/bjoc.8.80 doi (DE-627)DOAJ004208951 (DE-599)DOAJ14da70ba5b8e42869e3c50896eb2091b DE-627 ger DE-627 rakwb eng QD241-441 Christiane E. Kupper verfasserin aut Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry Ruben R. Rosencrantz verfasserin aut Birgit Henßen verfasserin aut Helena Pelantová verfasserin aut Stephan Thönes verfasserin aut Anna Drozdová verfasserin aut Vladimir Křen verfasserin aut Lothar Elling verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 712-725 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:712-725 https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b kostenfrei https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 712-725
allfieldsSound	10.3762/bjoc.8.80 doi (DE-627)DOAJ004208951 (DE-599)DOAJ14da70ba5b8e42869e3c50896eb2091b DE-627 ger DE-627 rakwb eng QD241-441 Christiane E. Kupper verfasserin aut Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry Ruben R. Rosencrantz verfasserin aut Birgit Henßen verfasserin aut Helena Pelantová verfasserin aut Stephan Thönes verfasserin aut Anna Drozdová verfasserin aut Vladimir Křen verfasserin aut Lothar Elling verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 712-725 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:712-725 https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b kostenfrei https://doi.org/10.3762/bjoc.8.80 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 712-725
language	English
source	In Beilstein Journal of Organic Chemistry 8(2012), 1, Seite 712-725 volume:8 year:2012 number:1 pages:712-725
sourceStr	In Beilstein Journal of Organic Chemistry 8(2012), 1, Seite 712-725 volume:8 year:2012 number:1 pages:712-725
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topic_facet	chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine Science Q Organic chemistry
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container_title	Beilstein Journal of Organic Chemistry
authorswithroles_txt_mv	Christiane E. Kupper @@aut@@ Ruben R. Rosencrantz @@aut@@ Birgit Henßen @@aut@@ Helena Pelantová @@aut@@ Stephan Thönes @@aut@@ Anna Drozdová @@aut@@ Vladimir Křen @@aut@@ Lothar Elling @@aut@@
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author	Christiane E. Kupper
spellingShingle	Christiane E. Kupper misc QD241-441 misc chemo-enzymatic synthesis misc galactose oxidase misc glycosyltransferase misc LacDiNAc misc poly-N-acetyllactosamine misc Science misc Q misc Organic chemistry Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
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topic_title	QD241-441 Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment chemo-enzymatic synthesis galactose oxidase glycosyltransferase LacDiNAc poly-N-acetyllactosamine
topic	misc QD241-441 misc chemo-enzymatic synthesis misc galactose oxidase misc glycosyltransferase misc LacDiNAc misc poly-N-acetyllactosamine misc Science misc Q misc Organic chemistry
topic_unstemmed	misc QD241-441 misc chemo-enzymatic synthesis misc galactose oxidase misc glycosyltransferase misc LacDiNAc misc poly-N-acetyllactosamine misc Science misc Q misc Organic chemistry
topic_browse	misc QD241-441 misc chemo-enzymatic synthesis misc galactose oxidase misc glycosyltransferase misc LacDiNAc misc poly-N-acetyllactosamine misc Science misc Q misc Organic chemistry
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hierarchy_parent_title	Beilstein Journal of Organic Chemistry
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title	Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
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title_full	Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
author_sort	Christiane E. Kupper
journal	Beilstein Journal of Organic Chemistry
journalStr	Beilstein Journal of Organic Chemistry
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lang_code	eng
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author_browse	Christiane E. Kupper Ruben R. Rosencrantz Birgit Henßen Helena Pelantová Stephan Thönes Anna Drozdová Vladimir Křen Lothar Elling
container_volume	8
class	QD241-441
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author-letter	Christiane E. Kupper
doi_str_mv	10.3762/bjoc.8.80
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title_sort	chemo-enzymatic modification of poly-n-acetyllactosamine (lacnac) oligomers and n,n-diacetyllactosamine (lacdinac) based on galactose oxidase treatment
callnumber	QD241-441
title_auth	Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
abstract	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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications.
abstractGer	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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications.
abstract_unstemmed	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; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]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. Product formation starting from different poly-LacNAc oligomers was characterised and optimised regarding formation of the C6-aldo product. Further modification of the aldehyde containing glycans, either by chemical conversion or enzymatic elongation, was established. Base-catalysed β-elimination, coupling of biotin–hydrazide with subsequent reduction to the corresponding hydrazine linkage, and coupling by reductive amination to an amino-functionalised poly-LacNAc oligomer were performed and the products characterised by LC–MS and NMR analysis. Remarkably, elongation of terminally oxidised poly-LacNAc glycans by β3GlcNAc- and β4Gal-transferase was also successful. In this way, a set of novel, modified poly-LacNAc oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications.
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title_short	Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
url	https://doi.org/10.3762/bjoc.8.80 https://doaj.org/article/14da70ba5b8e42869e3c50896eb2091b https://doaj.org/toc/1860-5397
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author2	Ruben R. Rosencrantz Birgit Henßen Helena Pelantová Stephan Thönes Anna Drozdová Vladimir Křen Lothar Elling
author2Str	Ruben R. Rosencrantz Birgit Henßen Helena Pelantová Stephan Thönes Anna Drozdová Vladimir Křen Lothar Elling
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doi_str	10.3762/bjoc.8.80
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up_date	2024-07-03T22:34:04.948Z
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Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

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