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 (1)H 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Crystallography, X-Ray
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Humans
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Lanthanoid Series Elements / chemistry*
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Conformation
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Organometallic Compounds / chemistry*
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Protons
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Quantum Theory
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Serum Albumin / chemistry*
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Stereoisomerism
Substances
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Lanthanoid Series Elements
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Organometallic Compounds
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Protons
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Serum Albumin