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

The enantioselective binding of the (SSS)-Delta 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 H-1 NMR spectrum relative to the (RRR)-Lambda 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.