Title : Site-specific PEGylation enhances the pharmacokinetic properties and antitumor activity of interferon beta-1b.

Pub. Date : 2013 Dec

PMID : 23962003






8 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Covalent modification of IFN-beta with polyethylene glycol (PEG) improves the pharmacokinetic properties of the protein, but can adversely affect the protein"s in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens
2 Covalent modification of IFN-beta with polyethylene glycol (PEG) improves the pharmacokinetic properties of the protein, but can adversely affect the protein"s in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens
3 Random modification of lysine residues in IFN-beta with amine-reactive PEGs decreased the in vitro bioactivity of the protein 50-fold, presumably due to modification of lysine residues near critical receptor binding sites. Polyethylene Glycols interferon beta 1 Homo sapiens
4 PEGylated IFN-beta proteins that retained high in vitro bioactivity could be obtained by selective modification of the N-terminus of the protein with PEG. Polyethylene Glycols interferon beta 1 Homo sapiens
5 Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens
6 Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens
7 Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens
8 Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity. Polyethylene Glycols interferon beta 1 Homo sapiens