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Protein and Protease Sensing by Allosteric Derepression
Hui Chin Goh1, Farid J Ghadessy2, Saurabh Nirantar1
1p53 Laboratory, A*STAR Agency for Science, Technology and Research, #06-04/05 Neuros, 138648, Singapore, Singapore.
Methods in Molecular Biology (Clifton, N.J.)
|March 16, 2017
Summary
We developed versatile sensors to detect protease activity and protein-peptide interactions. These tools enable screening for inhibitors using various output methods for cellular regulation studies.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Regulation
Background:
- Peptide motifs are essential for mediating protein-protein interactions.
- These motifs are also key sites for protease activity.
- Understanding these interactions and activities is vital for cellular regulation.
Purpose of the Study:
- To present novel, versatile, and modular sensors.
- To enable detection of protease activity.
- To facilitate the study of protein-peptide interactions and inhibitor screening.
Main Methods:
- Development of modular sensor platforms.
- Utilizing chromogenic, fluorescent, and luminescent output signals.
- Application in detecting protease activity and protein-peptide interactions.
Main Results:
- Demonstrated the versatility of the developed sensors.
- Successfully detected protease activity.
- Enabled screening for inhibitors of protein-peptide interactions.
Conclusions:
- The presented sensors offer a flexible approach for studying protease activity and protein-peptide interactions.
- These tools are valuable for identifying potential inhibitors.
- The modular design supports diverse applications in cellular regulation research.
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