DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Haeshin | ko |
dc.contributor.author | Jang, IH | ko |
dc.contributor.author | Ryu, SH | ko |
dc.contributor.author | Park, TG | ko |
dc.date.accessioned | 2009-11-23T08:25:18Z | - |
dc.date.available | 2009-11-23T08:25:18Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-05 | - |
dc.identifier.citation | PHARMACEUTICAL RESEARCH, v.20, no.5, pp.818 - 825 | - |
dc.identifier.issn | 0724-8741 | - |
dc.identifier.uri | http://hdl.handle.net/10203/13146 | - |
dc.description.abstract | Purpose. N-terminal site-specific mono-PEGylation of recombinant human epidermal growth factor (EGF) was accomplished using polyethyleneglycol ( PEG) derivatives (Mw = 2000 and 5000) through a reactive terminal aldehyde group. Methods. The site-specific PEG conjugation was conducted at a slightly acidic pH condition (pH 5.5). The mono-PEGylation was targeted to an alpha-amine group at the N-terminal end of EGF to minimize reduction of biologic activity. Tryptic digestion mapping and MALDI-TOF MS techniques were applied to show the occurrence of mono-PEGylation at the N-terminus of EGF. Results. The site-specific mono-PEGylated EGF, when compared with native EGF, fully retained its in vitro biologic activities such as cell proliferation and intracellular signal transduction. This revealed that although a synthetic polymer of a PEG was covalently conjugated to EGF, the internalized complex of PEGylated EGF-receptor within cells did not hamper the intracellular signal transduction events. The PEGylated EGF also exhibited a prolonged circulation in blood stream in vivo and markedly enhanced physical stability when incubated with tissue homogenate. Conclusion. N-terminally mono-PEGylated EGF shows increased physical stability while retaining its biologic activity. | - |
dc.description.sponsorship | DaeWoong Pharmaceutical Co. for the generous donation of EGF and Center for Advanced Functional Polymers, KAIST for the financial support | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | KLUWER ACADEMIC/PLENUM PUBL | - |
dc.subject | RECEPTOR TYROSINE KINASES | - |
dc.subject | POLYETHYLENE-GLYCOL | - |
dc.subject | DIRECTED MUTAGENESIS | - |
dc.subject | CELLS | - |
dc.subject | ENDOCYTOSIS | - |
dc.subject | EGF | - |
dc.subject | IMMUNOGENICITY | - |
dc.subject | MICROSPHERES | - |
dc.subject | CONJUGATION | - |
dc.subject | STABILITY | - |
dc.title | N-terminal site-specific mono-PEGylation of epidermal growth factor | - |
dc.type | Article | - |
dc.identifier.wosid | 000182446900017 | - |
dc.identifier.scopusid | 2-s2.0-0242584999 | - |
dc.type.rims | ART | - |
dc.citation.volume | 20 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | 818 | - |
dc.citation.endingpage | 825 | - |
dc.citation.publicationname | PHARMACEUTICAL RESEARCH | - |
dc.identifier.doi | 10.1023/A:1023402123119 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, Haeshin | - |
dc.contributor.localauthor | Park, TG | - |
dc.contributor.nonIdAuthor | Jang, IH | - |
dc.contributor.nonIdAuthor | Ryu, SH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | epidermal growth factor (EGF) | - |
dc.subject.keywordAuthor | poly(ethylene glycol) (PEG) | - |
dc.subject.keywordAuthor | site-specific PEGylation | - |
dc.subject.keywordAuthor | biologic activity | - |
dc.subject.keywordPlus | RECEPTOR TYROSINE KINASES | - |
dc.subject.keywordPlus | POLYETHYLENE-GLYCOL | - |
dc.subject.keywordPlus | DIRECTED MUTAGENESIS | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | ENDOCYTOSIS | - |
dc.subject.keywordPlus | EGF | - |
dc.subject.keywordPlus | IMMUNOGENICITY | - |
dc.subject.keywordPlus | MICROSPHERES | - |
dc.subject.keywordPlus | CONJUGATION | - |
dc.subject.keywordPlus | STABILITY | - |
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