A next-generation disulfide stapling reagent, incorporating both reducing and re-bridging functions, is shown to be successful across various proteins.
It has recently emerged that the succinimide linkage of a maleimide thiol addition product is fragile, which is a major issue in fields where thiol functionalisation needs to be robust. Herein we deliver a strategy that generates selective cysteine thiol labelling reagents, which are stable to hydrolysis and thiol exchange.
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