B3(Fab)-streptavidin tetramer has higher binding avidity than B3(scFv)-streptavidin tetramer

Jae Seon Won, Hye Won Kang, Pil Won Nam, Mu Hyeon Choe

Research output: Contribution to journalArticlepeer-review


Multivalent and multi-specific antibodies can provide valuable tools for bio-medical research, diagnosis and therapy. In antigen-antibody interactions, the avidity of antibodies depends on the affinity and the number of binding sites.1 As artificial multivalent antibody agents, single chain Fv-streptavidin fusion tetramer proteins (scFv-SA)4 have been previously tested.1,2 Although, the Fab domain is known to be more stable than scFv in animal models,3,4 it has never been used to make a multivalent agent with a streptavidin fusion. In this study, we prepared tetra-valent (Fab-cSA)4 by fusing Fab with core streptavidin (cSA). This molecule was made using inclusion body production, refolding and chromatography purification. Affinities of the Fab-cSA tetramer and a scFv-cSA tetramer to a cell surface antigen were compared by ELISA using biotin-HRP. The Fab-cSA tetramer showed higher binding avidity than the scFv-cSA tetramer. The higher binding avidity of the Fab-cSA tetramer demonstrates its potential as a therapeutic agent for target-specific antibody therapy.

Original languageEnglish
Pages (from-to)1101-1106
Number of pages6
JournalBulletin of the Korean Chemical Society
Issue number5
Publication statusPublished - 2009


  • Antibody therapy
  • Fab
  • Homo-tetramer
  • Recombinant antibody
  • Refolding

ASJC Scopus subject areas

  • General Chemistry


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