Issue 14, 2011

Enantioselective binding of a lanthanide(iii) complex to human serum albumin studied by 1H STD NMR techniques

Abstract

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 STD 1H NMR spectrum relative to the (RRR)-Λ isomer, by the effect of the competitive binder to that site, N-dansyl sarcosine, upon the STD spectrum of each isomer, in the presence of HSA and by 3D docking simulations.

Graphical abstract: Enantioselective binding of a lanthanide(iii) complex to human serum albumin studied by 1H STD NMR techniques

Supplementary files

Additions and corrections

Article information

Article type
Communication
Submitted
04 Apr 2011
Accepted
17 May 2011
First published
18 May 2011

Org. Biomol. Chem., 2011,9, 5047-5050

Enantioselective binding of a lanthanide(III) complex to human serum albumin studied by 1H STD NMR techniques

D. M. Dias, J. M. C. Teixeira, I. Kuprov, E. J. New, D. Parker and C. F. G. C. Geraldes, Org. Biomol. Chem., 2011, 9, 5047 DOI: 10.1039/C1OB05524K

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