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- W2045767384 abstract "Trichosanthin (TCS), a type I ribosome-inactivating protein (RIP), was modified with polyethylene glycol (PEG) in order to reduce its antigenicity and prolong its half-life. Computer modeling identified three potential antigenic sites namely Q219, K173 and S7. By site-directed mutagenesis, these sites were changed into cysteine through which PEG can be covalently attached. The resulting TCS had a PEG coupled directly above one of its potential antigenic determinants, hence masking the antigenic region and prevent binding of antibodies specific to this site. In general, mutation did not bring about significant changes in ribosome-inactivating activity, cytotoxicity, and abortifacient activity of TCS. However, the in vitro activities of PEG modified (PEGylated) TCS muteins were 3–20 folds lower and the in vivo activity 50% less than that of nTCS. Pharmacokinetics study indicated that all three PEGylated TCS muteins showed 6-fold increase in mean residence time as compared to unmodified muteins. The binding affinity of an IgE monoclonal antibody (TE1) to TCS was greatly reduced after PEG modification (PEGylation) at position Q219, suggesting that TE1 recognized an epitope very near to residue Q219. PEGylated TCS muteins induced similar IgG response but 4–16 fold lower IgE response in mice compared with nTCS." @default.
- W2045767384 created "2016-06-24" @default.
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- W2045767384 date "1999-02-01" @default.
- W2045767384 modified "2023-09-24" @default.
- W2045767384 title "Site-directed polyethylene glycol modification of trichosanthin: Effects on its biological activites, pharmacokinetics, and antigenicity" @default.
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- W2045767384 doi "https://doi.org/10.1016/s0024-3205(99)00048-x" @default.
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