Related Experiment Videos
Photoreversible antigen-antibody reactions.
1Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
FEBS Letters
|July 29, 1991
Summary
A new monoclonal antibody (Z1H01) binds a specific peptide only in its trans form. UV light causes the antibody to release the peptide, which it rebinds upon reversion to the trans form with visible light.
Area of Science:
- Biochemistry
- Immunology
- Photochemistry
Background:
- Monoclonal antibodies are crucial tools in biological research and diagnostics.
- Azobenzene-containing peptides can undergo photoisomerization between trans and cis forms.
- Controlling molecular interactions with light offers novel applications in biotechnology.
Purpose of the Study:
- To develop a photo-responsive antibody targeting an azobenzene-modified oligopeptide.
- To characterize the binding properties of the antibody in relation to the peptide's photoisomerization state.
- To explore the potential of light-controlled antibody-hapten interactions.
Main Methods:
- Preparation of a monoclonal antibody (Z1H01) against an azobenzene-functionalized oligopeptide in the trans configuration.
- Characterization of antibody-hapten binding affinity using equilibrium constants (K).
- Investigation of binding changes upon UV (trans to cis) and visible light (cis to trans) irradiation.
Main Results:
- The antibody exhibited strong binding to the hapten peptide in the trans form (K = 5 x 10(7) M-1).
- UV light induced isomerization to the cis form, leading to the release of the hapten from the antibody.
- Visible light promoted reversion to the trans form, restoring antibody-hapten binding.
Conclusions:
- The Z1H01 monoclonal antibody demonstrates light-switchable binding to its azobenzene-containing peptide hapten.
- This photo-responsive antibody system offers a mechanism for light-controlled molecular recognition.
- The findings open avenues for developing light-actuated biomolecular systems and drug delivery platforms.