Donor substrate binding to trans-sialidase of Trypanosoma cruzi as studied by STD NMR

Astrid Blume; Björn Neubacher; Joachim Thiem; Thomas Peters

doi:10.1016/j.carres.2007.05.037

Donor substrate binding to trans-sialidase of Trypanosoma cruzi as studied by STD NMR

Astrid Blume, Björn Neubacher, Joachim Thiem, Thomas Peters^*

^*Corresponding author for this work

Institute of Chemistry and Metabolomics

University of Hamburg

13 Citations (Scopus)

Abstract

Using STD NMR experiments, we have studied the binding epitopes of p-nitrophenyl glycosides of sialic acid and analogs thereof when bound to Trypanosoma cruzi trans-sialidase (TSia). Time-dependent NMR spectra yielded data on the rate of substrate hydrolysis in comparison to sialic acid transfer. Our experiments clearly demonstrate that shortening of the glycerol side chain significantly favors the transfer reaction over hydrolysis. Our results extend the basis on which specific trans-sialidase inhibitors may be designed.

Original language	English
Journal	Carbohydrate Research
Volume	342
Issue number	12-13
Pages (from-to)	1904-1909
Number of pages	6
ISSN	0008-6215
DOIs	https://doi.org/10.1016/j.carres.2007.05.037
Publication status	Published - 03.09.2007

Funding

T.P. and J.T. thank the Deutsche Forschungsgemeinschaft (DFG) for financial support within the project program grant SFB 470.

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.carres.2007.05.037

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title = "Donor substrate binding to trans-sialidase of Trypanosoma cruzi as studied by STD NMR",

abstract = "Using STD NMR experiments, we have studied the binding epitopes of p-nitrophenyl glycosides of sialic acid and analogs thereof when bound to Trypanosoma cruzi trans-sialidase (TSia). Time-dependent NMR spectra yielded data on the rate of substrate hydrolysis in comparison to sialic acid transfer. Our experiments clearly demonstrate that shortening of the glycerol side chain significantly favors the transfer reaction over hydrolysis. Our results extend the basis on which specific trans-sialidase inhibitors may be designed.",

author = "Astrid Blume and Bj{\"o}rn Neubacher and Joachim Thiem and Thomas Peters",

note = "Funding Information: T.P. and J.T. thank the Deutsche Forschungsgemeinschaft (DFG) for financial support within the project program grant SFB 470. Copyright: Copyright 2009 Elsevier B.V., All rights reserved.",

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doi = "10.1016/j.carres.2007.05.037",

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T1 - Donor substrate binding to trans-sialidase of Trypanosoma cruzi as studied by STD NMR

AU - Blume, Astrid

AU - Neubacher, Björn

AU - Thiem, Joachim

AU - Peters, Thomas

N1 - Funding Information: T.P. and J.T. thank the Deutsche Forschungsgemeinschaft (DFG) for financial support within the project program grant SFB 470. Copyright: Copyright 2009 Elsevier B.V., All rights reserved.

PY - 2007/9/3

Y1 - 2007/9/3

N2 - Using STD NMR experiments, we have studied the binding epitopes of p-nitrophenyl glycosides of sialic acid and analogs thereof when bound to Trypanosoma cruzi trans-sialidase (TSia). Time-dependent NMR spectra yielded data on the rate of substrate hydrolysis in comparison to sialic acid transfer. Our experiments clearly demonstrate that shortening of the glycerol side chain significantly favors the transfer reaction over hydrolysis. Our results extend the basis on which specific trans-sialidase inhibitors may be designed.

AB - Using STD NMR experiments, we have studied the binding epitopes of p-nitrophenyl glycosides of sialic acid and analogs thereof when bound to Trypanosoma cruzi trans-sialidase (TSia). Time-dependent NMR spectra yielded data on the rate of substrate hydrolysis in comparison to sialic acid transfer. Our experiments clearly demonstrate that shortening of the glycerol side chain significantly favors the transfer reaction over hydrolysis. Our results extend the basis on which specific trans-sialidase inhibitors may be designed.

UR - https://www.scopus.com/pages/publications/34447334814

U2 - 10.1016/j.carres.2007.05.037

DO - 10.1016/j.carres.2007.05.037

M3 - Journal articles

C2 - 17597593

AN - SCOPUS:34447334814

SN - 0008-6215

VL - 342

SP - 1904

EP - 1909

JO - Carbohydrate Research

JF - Carbohydrate Research

IS - 12-13

ER -

Donor substrate binding to trans-sialidase of Trypanosoma cruzi as studied by STD NMR

Abstract

Funding

Research Areas and Centers

UN SDGs

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