This study demonstrates an efficient palladium-catalyzed maleimidation process in peptides, suggesting strong chemoselectivity and broad substrate tolerance.
The incorporation of bioactive fragments or non-natural covalent linkages has shown to significantly improve the chemical stability and biological activity of peptides. In this study, we have developed a novel methodology for site-selective Pd-catalyzed maleimidation of phenylalanine-containing peptides. This synthetic strategy offers a straightforward and efficient approach for the construction of maleimide-phenylalanine covalent peptide conjugates. The merit of this method includes broad substrate tolerance, exclusive formation of Heck-type products, and excellent chemoselectivity.
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Tang et al. (2025) studied this question.
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