Related Experiment Videos
Phosphorylation-Responsive Membrane Transport of Peptides
Shu Peng1,2, Andrea Barba-Bon1, Yu-Chen Pan1,2
1Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.
Angewandte Chemie (International Ed. in English)
|October 13, 2017
Summary
Amphiphilic calixarenes enable supramolecular membrane transport systems responsive to peptide phosphorylation. These systems regulate kinase activity and allow label-free monitoring of protein kinase A (PKA) and protein kinase C (PKC) in biological signaling.
Area of Science:
- Biochemistry
- Supramolecular Chemistry
- Membrane Biology
Background:
- Kinase and phosphatase activity is crucial for biological signal transduction.
- Dysregulation of these enzymes is implicated in various diseases.
- Existing membrane transport systems lack phosphorylation responsiveness.
Purpose of the Study:
- To develop novel supramolecular membrane transport systems utilizing amphiphilic calixarenes.
- To investigate the phosphorylation-responsive transport capabilities of these systems.
- To enable label-free monitoring of kinase activity.
Main Methods:
- Dye-efflux experiments with liposomes.
- Utilizing amphiphilic calixarenes as counterion activators for cell-penetrating peptides.
- Testing transport of kinase substrates and their phosphorylated products.
Main Results:
- Calixarenes demonstrated high activity as counterion activators for cell-penetrating peptides (EC50 in low nanomolar range).
- Calixarenes facilitated membrane transport of kinase peptide substrates, but not their phosphorylated products.
- This differential transport allowed for regulation by protein kinase A (PKA) and protein kinase C (PKC).
Conclusions:
- Amphiphilic calixarenes are effective components for phosphorylation-responsive membrane transport.
- These systems offer a mechanism for regulating kinase activity and monitoring enzyme function.
- The developed system provides a label-free method for kinase assays.