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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 30, Number 5
BKCSDE 30(5)
May 20, 2009

Title	B3(Fab)-streptavidin Tetramer Has Higher Binding Avidity than B3(scFv)-streptavidin Tetramer
Author	Jae Seon Won, Hye Won Kang, Pil Won Nam, Mu Hyeon Choe*
Keywords	Recombinant antibody, Refolding, Fab, Homo-tetramer, Antibody therapy
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.
Page	1101 - 1106
Full Text	PDF

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