This methodology has been validated on peptides as well as protein insulin using a straightforward and mild condition. Herein, an approach to protein modification is described that relies on a photoredox method for the site-selective bioconjugation of phenylalanine. However, the covalent bioconjugation of native phenylalanine is one of the most challenging problems in protein modification. Only 3.8% natural abundance of phenylalanine in protein and nearly 90% of proteins contain at least one phenylalanine residue in their sequenced, showing the potential in biopharmaceutical utility of the phenylalanine bioconjugation. Site-selectively chemical bioconjugation of peptides and proteins can improve the therapeutic exploration of modified protein drugs.
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