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• W2725653208 abstract "In this article, ab initio calculations have been combined with a search in the Protein Data Bank (PDB) to demonstrate the importance of σ-hole tetrel bonding interactions in biological systems. In particular, we focus our attention on the ability of the -CF3 group to participate in noncovalent interactions as Lewis acids, and we show the importance of this interaction in the inhibition mechanism of a NADP+-dependent isocitrate dehydrogenase (IDH) enzyme that converts isocitrate to α-ketoglutarate. IDH mutations are found in multiple hematologic and solid tumors, inducing premalignant disorders. A potent triazine-based inhibitor of the mutant IDH (enasidenib) presents two -CF3 groups in the structure. One establishes a tetrel bonding interaction with an aspartate residue that contributes to the binding and selectivity of the inhibitor to the active site." @default.
• W2725653208 created "2017-07-14" @default.
• W2725653208 creator A5013755617 @default.
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• W2725653208 date "2017-07-11" @default.
• W2725653208 modified "2023-10-16" @default.
• W2725653208 title "Importance of R–CF₃···O Tetrel Bonding Interactions in Biological Systems" @default.
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• W2725653208 doi "https://doi.org/10.1021/acs.jpca.7b06052" @default.
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