Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1390841 | Carbohydrate Research | 2007 | 6 Pages |
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.
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Related Topics
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Authors
Astrid Blume, Björn Neubacher, Joachim Thiem, Thomas Peters,