Antibody Engineering Using Phage Display with a Coiled-Coil Heterodimeric Fv Antibody Fragment ccFv
2011
Antibody Engineering Using Phage Display with a Coiled-Coil Heterodimeric Fv Antibody Fragment ccFv
publication
Evidence: moderate
Author Information
Author(s): Wang Xinwei, Zhong Pinyu, Wang Kevin C.
Primary Institution: Merck Research Laboratories, Merck & Co., Inc.
Hypothesis
The study investigates the potential application of the ccFv antibody format in antibody engineering.
Conclusion
The ccFv antibody format shows comparable affinity and expressibility to scFv while demonstrating significantly better stability.
Supporting Evidence
- The ccFv molecule had a binding affinity similar to the corresponding scFv but was significantly improved in thermostability.
- Phage display libraries in the ccFv format were constructed for humanization and affinity maturation of the anti-VEGF antibody.
- The ccFv antibody exhibited significantly higher stability than the scFv antibody.
Takeaway
Scientists created a new type of antibody that is smaller and more stable, making it better for medical use.
Methodology
The study involved constructing a ccFv antibody, expressing it in Pichia pastoris, and comparing its stability and binding affinity to that of scFv antibodies.
Digital Object Identifier (DOI)
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