Abstract
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 language | English |
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Pages (from-to) | 1101-1106 |
Number of pages | 6 |
Journal | Bulletin of the Korean Chemical Society |
Volume | 30 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- Antibody therapy
- Fab
- Homo-tetramer
- Recombinant antibody
- Refolding
ASJC Scopus subject areas
- Chemistry(all)