High Affinity Antigen Recognition of the Dual Specific Variants of Herceptin Is Entropy-Driven in Spite of Structural Plasticity
2011
Understanding How Herceptin Variants Bind Two Different Antigens
publication
Evidence: high
Author Information
Author(s): Bostrom Jenny, Haber Lauric, Koenig Patrick, Kelley Robert F., Fuh Germaine
Primary Institution: Genentech Inc.
Hypothesis
How do dual specific variants of Herceptin bind to two unrelated protein antigens?
Conclusion
The study found that the dual specific antibody bH1 binds to both HER2 and VEGF with favorable entropy changes, despite its structural plasticity.
Supporting Evidence
- The dual specific antibody bH1 was engineered to bind both HER2 and VEGF.
- Binding interactions were characterized by favorable entropy changes.
- bH1 maintained many properties of Herceptin, including binding affinity and kinetics.
Takeaway
Scientists created a special antibody that can grab onto two different targets at once, and it does this without using up too much energy.
Methodology
The study involved engineering Herceptin to create dual specific antibodies, analyzing their binding properties using biophysical and thermodynamic methods.
Digital Object Identifier (DOI)
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