AI Article Synopsis
- The Fv fragment of the anti-lysozyme monoclonal antibody, HyHEL10, was stabilized by linking its variable domains with a flexible linker.
- Significant differences in expression levels were found between the two constructs (scFvHL and scFvLH) in E. coli, with scFvLH being more highly expressed and yielding 3-5 mg per liter of culture after purification.
- Although scFvLH showed an enthalpically favorable interaction with its antigen, HEL, it exhibited reduced binding activity due to entropic losses during binding.
Article Abstract
In order to physically stabilize the Fv fragment of anti-lysozyme monoclonal antibody, HyHEL10, the variable domains were linked covalently with a flexible linker. A marked difference in the level of expression in E. coli was observed between VH-linker-VL (scFvHL) and VL-linker-VH (scFvLH). The highly expressed scFvLH was purified by a single step of affinity chromatography from the culture supernatant with a typical yield of 3-5 mg per liter of culture. This HyHEL10 scFvLH showed reduced binding activity toward its antigen, HEL, in comparison with Fv. Thermodynamic study showed that this reduced activity was due to entropic loss upon binding to its antigen, although this interaction between scFvLH and its antigen was enthalpically favorable.
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