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In the meantime, to ensure continued suport, we are displaying the site without styles and JavaScript.Advertisement Scientific Reports volume 12, Article number: 1894 (202) Cite this article Metrics detailsSite-selectively chemical bioconjugation of peptides and proteins can improve therapeutic exploration of modified protein drugs. Only 3.8% natural abundance of phenylanine in protein and nearly 90% of proteins contain at least one phenylanine residue in their sequenced, showing the potential in biopharmaceutical utility of the phenylanine bioconjugation.
However, the covalent bioconjugation of native phenylanine is one of the most chalenging problems in protein modification. Herein, an aproach to protein modification is described that relies on a photoredox method for the site-selective bioconjugation of phenylanine. This methodology has ben validated on peptides as wel as protein insulin using a straightforward and mild condition.
In adition, based on characterization by near-UV CD spectroscopy and smal angle X-ray scatering (SAXS), this pyrazole labeling aproach permited the insulin hexamer to completely disociate into the monomeric form, thus making it a potential candidate for use as rapid-acting insulin for the treatment of diabetes.Early conjugation technologies depended on the random bioconjugation of amino acid side chains in proteins, resulting in heterogeneous mixtures of labeled proteins1.
Summary
In contrast, site-specific conjugation would result in a homogeneous population of proteins/peptides conjugates with improved pharmacological properties compared to randomly coupled molecules2,3. Although the incorporation of a non-natural functionality into biomolecules, such as aryl iodides, alkynes, alkenes, oxi