Abstract
Staying in the pocket: A cyclometalated iridium(III) biquinoline complex targets the protein-protein interface (see picture; C yellow, N blue, Ir dark green) of the tumor necrosis factor-α (TNF-α) trimer. Molecular-modeling studies confirm the nature of this interaction. Both enantiomers of the iridium complex display comparable in vitro potency to the strongest small-molecule inhibitor of TNF-α.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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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Coordination Complexes / chemistry*
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Crystallography, X-Ray
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Hep G2 Cells
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Humans
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Immobilized Proteins / antagonists & inhibitors
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Immobilized Proteins / metabolism
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Iridium / chemistry*
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Protein Interaction Maps
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Protein Structure, Tertiary
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Receptors, Tumor Necrosis Factor, Type I / antagonists & inhibitors
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Receptors, Tumor Necrosis Factor, Type I / metabolism
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Stereoisomerism
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Tumor Necrosis Factor-alpha / antagonists & inhibitors*
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Tumor Necrosis Factor-alpha / metabolism
Substances
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Coordination Complexes
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Immobilized Proteins
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Receptors, Tumor Necrosis Factor, Type I
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Tumor Necrosis Factor-alpha
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Iridium