B3(Fab)-streptavidin Tetramer Has Higher Binding Avidity than B3(scFv)-streptavidin Tetramer

Bulletin of the Korean chemical society

Mu Hyeon Choe¹  Pil Won Nam¹  Hye Won Kang¹  Jae Seon Won¹ 

关键词: Recombinant antibody;    Refolding;    Fab;    Homo-tetramer;    Antibody therapy;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

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.

【 授权许可】

Unknown