Preferential heterodimerization of a bispecific diabody based on a humanized anti-EGFR antibody 528

Ryutaro Asano, Yukiko Sone, Keiko Ikoma, Hiroki Hayashi, Takeshi Nakanishi, Mitsuo Umetsu, Yu Katayose, Michiaki Unno, Toshio Kudo, Izumi Kumagai

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

We report the utility of in vitro refolding in the preparation of monomorphous hEx3 bispecific diabodies with epidermal growth factor receptor and CD3 retargeting from insoluble aggregates in Escherichia coli. Appropriate interaction between cognate variable heavy and light chains led to the formation of functional hEx3 heterodimers in a diabody format rather than inactive homodimers. The refolded hEx3 was found to exhibit almost the equivalent activity to the hEx3 and single-chain hEx3 (hEx3-scDb) prepared in a mammalian secretion system. We suggest that the preparation of hEx3 from bacterial insoluble material by means of in vitro refolding would be useful for industrial-scale production of the diabody for its potential use in clinical studies.

Original languageEnglish
Pages (from-to)597-603
Number of pages7
JournalProtein Engineering, Design and Selection
Volume21
Issue number10
DOIs
Publication statusPublished - 2008 Oct

Keywords

  • Bispecific diabody
  • Cancer immunotherapy
  • EGFR
  • In vitro refolding
  • Small recombinant antibody

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Molecular Biology

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