Mix to validate: A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo

Tae Hyung Kim, Magdalena Swierczewska, Yumin Oh, Aeryon Kim, Dong Gyu Jo, Jae Hyung Park, Youngro Byun, Scheherazade Sadegh-Nasseri, Martin G. Pomper, Kang Choon Lee, Seulki Lee

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ complex of nitrilotriacetic acid (NTA, see picture), a well-established practice in protein research, was used to improve the half-life of therapeutic proteins in the blood following systemic administration in vivo. Animal models show that this site-specific modification improves the efficacy of modified TRAIL proteins.

Original languageEnglish (US)
Pages (from-to)6880-6884
Number of pages5
JournalAngewandte Chemie - International Edition
Volume52
Issue number27
DOIs
StatePublished - Jul 1 2013

Keywords

  • PEGylation
  • drug screening
  • histidine tags
  • protein design
  • protein modifications

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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