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dc.contributor.authorShaunak, Sunil
dc.contributor.authorGodwin, Antony
dc.contributor.authorChoi, Ji-Won
dc.contributor.authorBalan, Sibu
dc.contributor.authorPedone, Elisa
dc.contributor.authorVijayarangam, Damotharan
dc.contributor.authorHeidelberger, Sibylle
dc.contributor.authorTeo, Ian
dc.contributor.authorZloh, Mire
dc.contributor.authorBrocchini, Steve
dc.date.accessioned2013-08-22T12:30:01Z
dc.date.available2013-08-22T12:30:01Z
dc.date.issued2006
dc.identifier.citationShaunak , S , Godwin , A , Choi , J-W , Balan , S , Pedone , E , Vijayarangam , D , Heidelberger , S , Teo , I , Zloh , M & Brocchini , S 2006 , ' Site-specific PEGylation of native disulfide bonds in therapeutic proteins ' , Nature Chemical Biology , vol. 2 , no. 6 , pp. 312-3 . https://doi.org/10.1038/nchembio786
dc.identifier.issn1552-4450
dc.identifier.otherPURE: 1458136
dc.identifier.otherPURE UUID: 185f1a1a-0412-430c-b0ae-f9321b9fd08d
dc.identifier.otherPubMed: 16633351
dc.identifier.otherScopus: 33646863688
dc.identifier.urihttp://hdl.handle.net/2299/11452
dc.description.abstractNative 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.en
dc.format.extent2
dc.language.isoeng
dc.relation.ispartofNature Chemical Biology
dc.titleSite-specific PEGylation of native disulfide bonds in therapeutic proteinsen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted2006
rioxxterms.versionofrecordhttps://doi.org/10.1038/nchembio786
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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