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 |
|---|---|
| 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 Oct 13 |
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Keywords
- Antibody therapy
- Fab
- Homo-tetramer
- Recombinant antibody
- Refolding
ASJC Scopus subject areas
- Chemistry(all)
Cite this
B3(Fab)-streptavidin tetramer has higher binding avidity than B3(scFv)-streptavidin tetramer. / Won, Jae Seon; Kang, Hye Won; Nam, Pil Won; Choe, MuHyeon.
In: Bulletin of the Korean Chemical Society, Vol. 30, No. 5, 13.10.2009, p. 1101-1106.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - B3(Fab)-streptavidin tetramer has higher binding avidity than B3(scFv)-streptavidin tetramer
AU - Won, Jae Seon
AU - Kang, Hye Won
AU - Nam, Pil Won
AU - Choe, MuHyeon
PY - 2009/10/13
Y1 - 2009/10/13
N2 - 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.
AB - 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.
KW - Antibody therapy
KW - Fab
KW - Homo-tetramer
KW - Recombinant antibody
KW - Refolding
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UR - http://www.scopus.com/inward/citedby.url?scp=70349752071&partnerID=8YFLogxK
U2 - 10.5012/bkcs.2009.30.5.1101
DO - 10.5012/bkcs.2009.30.5.1101
M3 - Article
AN - SCOPUS:70349752071
VL - 30
SP - 1101
EP - 1106
JO - Bulletin of the Korean Chemical Society
JF - Bulletin of the Korean Chemical Society
SN - 0253-2964
IS - 5
ER -