TY - JOUR
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 - http://www.scopus.com/inward/record.url?scp=34447334814&partnerID=8YFLogxK
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 -
