| Autor: |
Shaunak, Sunil, Godwin, Antony, Ji-Won Choi, Balan, Sibu, Pedone, Elisa, Vijayarangam, Damotharan, Heidelberger, Sibylle, Teo, Ian, Zloh, Mire, Brocchini, Steve |
| Předmět: |
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| Zdroj: |
Nature Chemical Biology; Jun2006, Vol. 2 Issue 6, p312-313, 2p, 2 Graphs |
| Abstrakt: |
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 α-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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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