ArticleResearch in pharmaceutical sciences2026
Enhancing soluble expression and purification of a bispecific scFv antibody in
Article in Research in pharmaceutical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background and purpose: The use of a bispecific antibody engineered as a tandem single-chain fragment variable antibody (scFv-BsAb) offers several advantages over full-length antibodies, including enhanced tissue penetration and the potential for production in bacterial cells. However, production of them in bacteria usually results in the formation of inclusion bodies. The current work aimed to facilitate proper folding and soluble expression of a recombinant scFv-BsAb targeting cytotoxic T-lymphocyte-associated protein 4 (CTLA-4) and programmed cell death protein 1 (PD-1) by co-expression with molecular chaperones. Experimental approach: Findings/Results: Co-expression with chaperones slightly enhanced the expression of soluble scFv-BsAb. The optimal condition for soluble expression of protein is at a temperature of 30 °C and an IPTG concentration of 1 mM when co-expressed with chaperones. The final yield of protein in co-expression with chaperones was 2.9 mg protein per 1 L of culture. Conclusion and implications: Optimization of culture conditions and co-expression with molecular chaperones may be useful for the production of soluble and functionally bioactive scFv antibodies in
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