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Department of Life Sciences and Center of Neurosciences and Cell Biology, Faculty of Science and Technology, University of Coimbra, P.O. Box 3046, 3001-401 Coimbra, Portugal
E-mail: geraldes@bioq.uc.pt
b
Department of Chemistry, Durham University, South Road, Durham, UK
E-mail: david.parker@durham.ac.uk
Org. Biomol. Chem., 2011,9, 5047-5050
DOI:
10.1039/C1OB05524K
Received
04 Apr 2011,
Accepted
17 May 2011
First published online
18 May 2011
The enantioselective binding of the (SSS)-Δ isomer of an yttrium(III) tetraazatriphenylene complex to ‘drug-site II’ of human serum albumin (HSA) was detected by the intensity differences of its STD1H NMR spectrum relative to the (RRR)-Λ isomer, by the effect of the competitive binder to that site, N-dansyl sarcosine, upon the STDspectrum of each isomer, in the presence of HSA and by 3D docking simulations.
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Organic & Biomolecular Chemistry
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