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Synthesis of peptides and proteins containing multiple disulfide bonds is challenging, limiting the elucidation of their biological functions. Here, the authors report a general synthetic strategy for fast formation of two and three disulfide bonds in peptides and proteins, and apply it to prepare several therapeutically important peptides.

Cysteine side chains are reactive sites of protein synthesis and modification. Here, the authors show that tuning palladium chemoselectivity allows for selective removal of several cysteine protection groups, and use their method to synthesize challenging protein analogues.