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Issue 23, 2003
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Exploring the active site of human factor Xa protein by NMR screening of small molecule probes

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Abstract

A collection of small molecules (MW < 350 Da) was screened for binding to human factor Xa using saturation transfer difference NMR spectroscopy to detect binding. The NMR screening experiments identified four hits. Binding isotherms constructed from NMR linewidth data showed that the binding affinities of the hits were all in the 30–210 µM range. Competition binding experiments showed that three of the ligands were displaced by a known μM inhibitor of factor Xa. The success of the method for identifying new ligands and the relevance of this information to the design of new factor Xa inhibitors are discussed.

Graphical abstract: Exploring the active site of human factor Xa protein by NMR screening of small molecule probes

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Publication details

The article was received on 26 Aug 2003, accepted on 13 Oct 2003 and first published on 31 Oct 2003


Article type: Paper
DOI: 10.1039/B310265C
Citation: Org. Biomol. Chem., 2003,1, 4235-4241

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    Exploring the active site of human factor Xa protein by NMR screening of small molecule probes

    L. Fielding, D. Fletcher, S. Rutherford, J. Kaur and J. Mestres, Org. Biomol. Chem., 2003, 1, 4235
    DOI: 10.1039/B310265C

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