FEBS Letters | |
A dimeric bispecific miniantibody combines two specificities with avidity | |
Müller, Kristian M.1  Arndt, Katja M.1  Plückthun, Andreas1  | |
[1] Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, CH-8050 Zürich, Switzerland | |
关键词: Protein design; Dimerization domain; Bispecific antibody; scFv fragment; 425; anti-EGF-receptor scFv; dhlx; helix-turn-helix dimerization domain; DiBi; dimeric bispecific; EGF-R; epidermal growth factor receptor; FITC-E2; anti-fluorescein scFv; IMAC; immobilized metal ion affinity chromatography; PC; phosphorylcholine; RU; resonance units; M1; anti-CD2 scFv; scFv; single-chain Fv fragment of an antibody; | |
DOI : 10.1016/S0014-5793(98)00829-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Bispecific antibodies extend the capabilities of nature and might be applied in immunotherapy and biotechnology. By fusing the gene of a single-chain Fv (scFv) fragment to a helical dimerization domain, followed by a second scFv fragment of different specificity, we were able to express a functional protein in E. coli, which is bispecific and has two valencies for each specificity. The dimeric bispecific (DiBi) miniantibody preserves the natural avidity of antibodies in a very small-sized molecule of only 120 kDa. The generality of the principle was shown with a scFv fragment binding the EGF-receptor (named scFv 425) in three combinations with scFv fragments either directed against CD2 (ACID2.M1), phosphorylcholine (McPC603) or fluorescein (FITC-E2). Binding was analyzed by sandwich surface plasmon resonance biosensor (BIAcore) measurements.
【 授权许可】
Unknown
【 预 览 】
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