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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Chemie und Metabolomics

Universität Hamburg

13 Zitate (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.

Originalsprache	Englisch
Zeitschrift	Carbohydrate Research
Jahrgang	342
Ausgabenummer	12-13
Seiten (von - bis)	1904-1909
Seitenumfang	6
ISSN	0008-6215
DOIs	https://doi.org/10.1016/j.carres.2007.05.037
Publikationsstatus	Veröffentlicht - 03.09.2007

Fördermittel

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

UN SDGs

Dieser Output leistet einen Beitrag zu folgendem(n) Ziel(en) für nachhaltige Entwicklung

SDG 3 – Gesundheit und Wohlergehen

Strategische Forschungsbereiche und Zentren

Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

Dokumente

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",

language = "English",

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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

Fördermittel

UN SDGs

Strategische Forschungsbereiche und Zentren

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