Brief Communication abstract
Nature Chemical Biology 2, 312 - 313 (2006)
Published online: 23 April 2006 | doi:10.1038/nchembio786
Site-specific PEGylation of native disulfide bonds in therapeutic proteins
Sunil Shaunak1, Antony Godwin2, Ji-Won Choi1, Sibu Balan2, Elisa Pedone2, Damotharan Vijayarangam1, Sibylle Heidelberger3, Ian Teo1, Mire Zloh3 & Steve Brocchini2
Native disulfide bonds in therapeutic proteins are crucial for tertiary structure and biological activity and are therefore considered unsuitable for chemical modification1, 2. We show that native disulfides in human interferon 
-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.
- Faculty of Medicine, Imperial College London, Hammersmith Hospital, Ducane Road, London W12 0NN, UK.
- Department of Pharmaceutics, The School of Pharmacy, University of London, 29/39 Brunswick Square, London WC1N 1AX, UK.
- Department of Pharmaceutical and Biological Chemistry, The School of Pharmacy, University of London, 29/39 Brunswick Square, London WC1N 1AX, UK.
Correspondence to: Sunil Shaunak1 e-mail: s.shaunak@imperial.ac.uk
Correspondence to: Steve Brocchini2 e-mail: steve.brocchini@pharmacy.ac.uk
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Site-specific PEGylation of native disulfide bonds in therapeutic proteinsNature Chemical Biology Brief Communication (01 Jun 2006)
