Traditional approaches to covalent drug design postulate that noncovalent binding affinity (K i) should be in the nanomolar range for the lead compound to be attractive. A study by Hansen et al. suggests that covalent K-Ras inhibitors can have weak noncovalent binding affinity yet have fast chemical reactivity (k inact), because K-Ras enhances the covalent reactivity of bound inhibitor, similarly to how enzymes activate their substrates.
Nature Structural & Molecular Biology – Springer Journals
Published: May 14, 2018
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