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Covalent inhibitors : an opportunity for rational target selectivity

Published in Current opinion in chemical biology. 2017, vol. 39, p. 54-63
Abstract There is a resurging interest in compounds that engage their target through covalent interactions. Cysteine's thiol is endowed with enhanced reactivity, making it the nucleophile of choice for covalent engagement with a ligand aligning an electrophilic trap with a cysteine residue in a target of interest. The paucity of cysteine in the proteome coupled to the fact that closely related proteins do not necessarily share a given cysteine residue enable a level of unprecedented rational target selectivity. The recent demonstration that a lysine's amine can also be engaged covalently with a mild electrophile extends the potential of covalent inhibitors. The growing database of protein structures facilitates the discovery of covalent inhibitors while the advent of proteomic technologies enables a finer resolution in the selectivity of covalently engaged proteins. Here, we discuss recent examples of discovery and design of covalent inhibitors.
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Research group Groupe Winssinger
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LAGOUTTE, Roman, PATOURET, Rémi, WINSSINGER, Nicolas. Covalent inhibitors : an opportunity for rational target selectivity. In: Current opinion in chemical biology, 2017, vol. 39, p. 54-63. doi: 10.1016/j.cbpa.2017.05.008 https://archive-ouverte.unige.ch/unige:95268

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Deposited on : 2017-07-04

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