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Site-selective covalent reactions on proteinogenic amino acids

So, Wing Ho, Zhang, Yu, Kang, Wei, Wong, Clarence T.T., Sun, Hongyan and Xia, Jiang 2017. Site-selective covalent reactions on proteinogenic amino acids. Current Opinion in Biotechnology 48 , pp. 220-227. 10.1016/j.copbio.2017.06.003

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To achieve precise control of the signaling events or to achieve unmistakable synthesis of biomolecules, nature has evolved organic reactions involving proteinogenic amino acids with unparalleled site selectivity. For example, dedicated enzymes accurately dictate the site of post-translational modifications in signaling proteins, and ribosomes precisely link the C-terminal carboxylic acid of one unprotected amino acid with the N-terminal amino group of the other amino acid through spatially confined proximity. For many years, chemists have been striving to achieve site selectivity on biomolecules by mimicking nature. Driven by the development of chemoselective protein conjugation reactions, enzymology and protein–protein interactions, the past decade has witnessed a boom in site-selective protein conjugation reactions. (In this review, a site-selective protein conjugation reaction is defined as an organic reaction that targets a single amino acid instead of a kind of amino acids in a protein or a proteome under physiological conditions, for example, a single cysteine residue among all of the cysteines.) In this review, we summarize the recent advancements of bioconjugation reactions that demonstrate this feature of precise site selectivity, focusing on the reactions of the proteinogenic amino acids (excluding those at non-coded or non-proteinogenic amino acids that are introduced to proteins through genetic manipulations).

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Publisher: Elsevier
ISSN: 0958-1669
Last Modified: 27 May 2021 14:30

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