Answers are grounded in this paper and cite their sources.
Demonstrates chemoselective modification of peptides and proteins at cysteine, indicating improved bioconjugate synthesis.
The modification of peptides and proteins has emerged as a powerful means to efficiently prepare high value bioconjugates for a range of applications in chemical biology and for the development of next-generation therapeutics. Herein, we report a novel method for the chemoselective late-stage modification of peptides and proteins at cysteine in aqueous buffer with suitably functionalised diaryliodonium salts, furnishing stable thioether-linked synthetic conjugates. The power of this new platform is showcased through the late-stage modification of the affibody zEGFR and the histone protein H2A.
No takes yet. Share an insight, caveat, or question.
Byrne et al. (2021) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: