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        Site-specific PEGylation of native disulfide bonds in therapeutic proteins

        Author
        Shaunak, Sunil
        Godwin, Antony
        Choi, Ji-Won
        Balan, Sibu
        Pedone, Elisa
        Vijayarangam, Damotharan
        Heidelberger, Sibylle
        Teo, Ian
        Zloh, Mire
        Brocchini, Steve
        Attention
        2299/11452
        Abstract
        Native disulfide bonds in therapeutic proteins are crucial for tertiary structure and biological activity and are therefore considered unsuitable for chemical modification. We show that native disulfides in human interferon alpha-2b and in a fragment of an antibody to CD4(+) can be modified by site-specific bisalkylation of the two cysteine sulfur atoms to form a three-carbon PEGylated bridge. The yield of PEGylated protein is high, and tertiary structure and biological activity are retained.
        Publication date
        2006
        Published in
        Nature Chemical Biology
        Published version
        https://doi.org/10.1038/nchembio786
        Other links
        http://hdl.handle.net/2299/11452
        Relations
        School of Life and Medical Sciences
        Metadata
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