Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography
The synthesis of multivalent sialylated glycoclusters is herein addressed by a chemoenzymatic approach using the trans-sialidase of Trypanosoma cruzi (TcTS). Multivalent β-thio-galactopyranosides and β-thio-lactosides were used as acceptor substrates and 3′-sialyllactose as the sialic acid donor. Hi...
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2016
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02820080_v33_n5_p809_AgustA http://hdl.handle.net/20.500.12110/paper_02820080_v33_n5_p809_AgustA |
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paper:paper_02820080_v33_n5_p809_Agusti2023-06-08T15:27:00Z Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography Cagnoni, Alejandro J. Kovensky, José Eduardo Muchnik de Lederkremer, Rosa María Uhrig, María Laura Enzymatic sialylation HPAEC MALDI-TOF Multivalent glycoclusters Sialic acid T. cruzi trans-sialidase β-galactopyranosides beta thio glycocluster carbohydrate derivative glycan n acetyllactosamine sialic acid derivative sialidase unclassified drug glycoprotein lactose N-acetylneuraminoyllactose protozoal protein sialidase thioglycoside trans-sialidase analytic method anion exchange chromatography Article catalysis chemical structure enzyme activity high performance anion exchange chromatography matrix-assisted laser desorption-ionization mass spectrometry nonhuman priority journal sialylation Trypanosoma cruzi analogs and derivatives chemistry enzymology high performance liquid chromatography Trypanosoma cruzi Chromatography, High Pressure Liquid Glycoproteins Lactose Neuraminidase Protozoan Proteins Sialic Acids Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Thiogalactosides Trypanosoma cruzi The synthesis of multivalent sialylated glycoclusters is herein addressed by a chemoenzymatic approach using the trans-sialidase of Trypanosoma cruzi (TcTS). Multivalent β-thio-galactopyranosides and β-thio-lactosides were used as acceptor substrates and 3′-sialyllactose as the sialic acid donor. High performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) was shown to be an excellent technique for the analysis of the reaction products. Different eluting conditions were optimized to allow the simultaneous resolution of the sialylated species, as well as their neutral precursors. The TcTS efficiently transferred sialyl residues to di, tri, tetra and octa β-thiogalactosides. In the case of an octavalent thiolactoside, up to six polysialylated compounds could be resolved. Preparative sialylation reactions were performed using the tetravalent and octavalent acceptor substrates. The main sialylated derivatives could be unequivocally assigned by MALDI mass spectrometry. Inhibition of the transfer to the natural substrate, N-acetyllactosamine, was also studied. The octalactoside caused 82 % inhibition of sialic acid transfer when we used equimolar concentrations of donor, acceptor and inhibitor. © 2016, Springer Science+Business Media New York. Fil:Cagnoni, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kovensky, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:de Lederkremer, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Uhrig, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02820080_v33_n5_p809_AgustA http://hdl.handle.net/20.500.12110/paper_02820080_v33_n5_p809_AgustA |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Enzymatic sialylation HPAEC MALDI-TOF Multivalent glycoclusters Sialic acid T. cruzi trans-sialidase β-galactopyranosides beta thio glycocluster carbohydrate derivative glycan n acetyllactosamine sialic acid derivative sialidase unclassified drug glycoprotein lactose N-acetylneuraminoyllactose protozoal protein sialidase thioglycoside trans-sialidase analytic method anion exchange chromatography Article catalysis chemical structure enzyme activity high performance anion exchange chromatography matrix-assisted laser desorption-ionization mass spectrometry nonhuman priority journal sialylation Trypanosoma cruzi analogs and derivatives chemistry enzymology high performance liquid chromatography Trypanosoma cruzi Chromatography, High Pressure Liquid Glycoproteins Lactose Neuraminidase Protozoan Proteins Sialic Acids Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Thiogalactosides Trypanosoma cruzi |
| spellingShingle |
Enzymatic sialylation HPAEC MALDI-TOF Multivalent glycoclusters Sialic acid T. cruzi trans-sialidase β-galactopyranosides beta thio glycocluster carbohydrate derivative glycan n acetyllactosamine sialic acid derivative sialidase unclassified drug glycoprotein lactose N-acetylneuraminoyllactose protozoal protein sialidase thioglycoside trans-sialidase analytic method anion exchange chromatography Article catalysis chemical structure enzyme activity high performance anion exchange chromatography matrix-assisted laser desorption-ionization mass spectrometry nonhuman priority journal sialylation Trypanosoma cruzi analogs and derivatives chemistry enzymology high performance liquid chromatography Trypanosoma cruzi Chromatography, High Pressure Liquid Glycoproteins Lactose Neuraminidase Protozoan Proteins Sialic Acids Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Thiogalactosides Trypanosoma cruzi Cagnoni, Alejandro J. Kovensky, José Eduardo Muchnik de Lederkremer, Rosa María Uhrig, María Laura Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| topic_facet |
Enzymatic sialylation HPAEC MALDI-TOF Multivalent glycoclusters Sialic acid T. cruzi trans-sialidase β-galactopyranosides beta thio glycocluster carbohydrate derivative glycan n acetyllactosamine sialic acid derivative sialidase unclassified drug glycoprotein lactose N-acetylneuraminoyllactose protozoal protein sialidase thioglycoside trans-sialidase analytic method anion exchange chromatography Article catalysis chemical structure enzyme activity high performance anion exchange chromatography matrix-assisted laser desorption-ionization mass spectrometry nonhuman priority journal sialylation Trypanosoma cruzi analogs and derivatives chemistry enzymology high performance liquid chromatography Trypanosoma cruzi Chromatography, High Pressure Liquid Glycoproteins Lactose Neuraminidase Protozoan Proteins Sialic Acids Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Thiogalactosides Trypanosoma cruzi |
| description |
The synthesis of multivalent sialylated glycoclusters is herein addressed by a chemoenzymatic approach using the trans-sialidase of Trypanosoma cruzi (TcTS). Multivalent β-thio-galactopyranosides and β-thio-lactosides were used as acceptor substrates and 3′-sialyllactose as the sialic acid donor. High performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) was shown to be an excellent technique for the analysis of the reaction products. Different eluting conditions were optimized to allow the simultaneous resolution of the sialylated species, as well as their neutral precursors. The TcTS efficiently transferred sialyl residues to di, tri, tetra and octa β-thiogalactosides. In the case of an octavalent thiolactoside, up to six polysialylated compounds could be resolved. Preparative sialylation reactions were performed using the tetravalent and octavalent acceptor substrates. The main sialylated derivatives could be unequivocally assigned by MALDI mass spectrometry. Inhibition of the transfer to the natural substrate, N-acetyllactosamine, was also studied. The octalactoside caused 82 % inhibition of sialic acid transfer when we used equimolar concentrations of donor, acceptor and inhibitor. © 2016, Springer Science+Business Media New York. |
| author |
Cagnoni, Alejandro J. Kovensky, José Eduardo Muchnik de Lederkremer, Rosa María Uhrig, María Laura |
| author_facet |
Cagnoni, Alejandro J. Kovensky, José Eduardo Muchnik de Lederkremer, Rosa María Uhrig, María Laura |
| author_sort |
Cagnoni, Alejandro J. |
| title |
Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| title_short |
Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| title_full |
Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| title_fullStr |
Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| title_full_unstemmed |
Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| title_sort |
multivalent sialylation of β-thio-glycoclusters by trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography |
| publishDate |
2016 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02820080_v33_n5_p809_AgustA http://hdl.handle.net/20.500.12110/paper_02820080_v33_n5_p809_AgustA |
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