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dc.contributor.authorBrocchini, Steve
dc.contributor.authorBalan, Sibu
dc.contributor.authorGodwin, Antony
dc.contributor.authorChoi, Ji-Won
dc.contributor.authorZloh, Mire
dc.contributor.authorShaunak, Sunil
dc.identifier.citationBrocchini , S , Balan , S , Godwin , A , Choi , J-W , Zloh , M & Shaunak , S 2006 , ' PEGylation of native disulfide bonds in proteins ' , Nature Protocols , vol. 1 , no. 5 , pp. 2241-52 .
dc.identifier.otherPURE: 1457917
dc.identifier.otherPURE UUID: 957da04c-f11f-4569-a14f-46695cfa5bf2
dc.identifier.otherPubMed: 17406463
dc.identifier.otherScopus: 33846987785
dc.description.abstractPEGylation has turned proteins into important new biopharmaceuticals. The fundamental problems with the existing approaches to PEGylation are inefficient conjugation and the formation of heterogeneous mixtures. This is because poly(ethylene glycol) (PEG) is usually conjugated to nucleophilic amine residues. Our PEGylation protocol solves these problems by exploiting the chemical reactivity of both of the sulfur atoms in the disulfide bond of many biologically relevant proteins. An accessible disulfide bond is mildly reduced to liberate the two cysteine sulfur atoms without disturbing the protein's tertiary structure. Site-specific PEGylation is achieved with a bis-thiol alkylating PEG reagent that sequentially undergoes conjugation to form a three-carbon bridge. The two sulfur atoms are re-linked with PEG selectively conjugated to the bridge. PEGylation of a protein can be completed in 24 h and purification of the PEG-protein conjugate in another 3 h. We have successfully applied this approach to PEGylation of cytokines, enzymes, antibody fragments and peptides, without destroying their tertiary structure or abolishing their biological activity.en
dc.relation.ispartofNature Protocols
dc.titlePEGylation of native disulfide bonds in 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
rioxxterms.typeJournal Article/Review

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