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Abstract:

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.

Registro:

Documento: Artículo
Título:Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography
Autor:Agustí, R.; Cano, M.E.; Cagnoni, A.J.; Kovensky, J.; de Lederkremer, R.M.; Uhrig, M.L.
Filiación:CIHIDECAR-CONICET, Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, Buenos Aires, 1428, Argentina
Laboratoire de Glycochimie, des Antimicrobiens et des Agroressources (LG2A)-CNRS UMR 7478, Université de Picardie Jules Verne, 33 rue Saint Leu, Amiens Cedex, 80039, France
Palabras clave: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
Año:2016
Volumen:33
Número:5
Página de inicio:809
Página de fin:818
DOI: http://dx.doi.org/10.1007/s10719-016-9676-0
Título revista:Glycoconjugate Journal
Título revista abreviado:Glycoconjugate J.
ISSN:02820080
CODEN:GLJOE
CAS:sialidase, 9001-67-6; lactose, 10039-26-6, 16984-38-6, 63-42-3, 64044-51-5; Glycoproteins; Lactose; N-acetylneuraminoyllactose; Neuraminidase; Protozoan Proteins; Sialic Acids; Thiogalactosides; trans-sialidase
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02820080_v33_n5_p809_AgustA­

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Citas:

---------- APA ----------
Agustí, R., Cano, M.E., Cagnoni, A.J., Kovensky, J., de Lederkremer, R.M. & Uhrig, M.L. (2016) . Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography. Glycoconjugate Journal, 33(5), 809-818.
http://dx.doi.org/10.1007/s10719-016-9676-0
---------- CHICAGO ----------
Agustí, R., Cano, M.E., Cagnoni, A.J., Kovensky, J., de Lederkremer, R.M., Uhrig, M.L. "Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography" . Glycoconjugate Journal 33, no. 5 (2016) : 809-818.
http://dx.doi.org/10.1007/s10719-016-9676-0
---------- MLA ----------
Agustí, R., Cano, M.E., Cagnoni, A.J., Kovensky, J., de Lederkremer, R.M., Uhrig, M.L. "Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography" . Glycoconjugate Journal, vol. 33, no. 5, 2016, pp. 809-818.
http://dx.doi.org/10.1007/s10719-016-9676-0
---------- VANCOUVER ----------
Agustí, R., Cano, M.E., Cagnoni, A.J., Kovensky, J., de Lederkremer, R.M., Uhrig, M.L. Multivalent sialylation of β-thio-glycoclusters by Trypanosoma cruzi trans sialidase and analysis by high performance anion exchange chromatography. Glycoconjugate J. 2016;33(5):809-818.
http://dx.doi.org/10.1007/s10719-016-9676-0