Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study |
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Authors: | Ludwig Nissler Rolf Gebhardt Stefan Berger |
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Institution: | (1) Institute of Biochemistry, Medical Faculty, University of Leipzig, Liebigstrasse 16, 04103 Leipzig, Germany;(2) Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, 04103 Leipzig, Germany |
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Abstract: | Flavonoids are well known to inhibit the function of the multi-drug-resistance (mdr) transporter by interacting with their ATP binding domains. The precise orientation of these molecules inside the ATP binding pocket is still unclear. We applied the saturation transfer difference (STD) NMR technique to investigate the binding of the flavonoid luteolin and its 7-O--D-glycopyranoside to the recombinant nucleotide binding domain (NBD2) of mouse-mdr. First, this NMR technique confirmed binding of both ligands to NBD2, as was determined from tryptophan fluorescence-quenching experiments. Further, the results suggest binding of both luteolin and its 7-O--D-glycopyranoside by their polar groups at positions 4, 5, and 3 to the protein.Abbreviations pgp
p-Glycoprotein
- NBD2
C-Terminal nucleotide binding domain of mouse multi drug resistance protein (mdr) |
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Keywords: | ATP binding pocket Flavonoids Multi-drug-resistance protein Protein– ligand interaction STD-NMR technique |
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