Abstract
The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled-coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled-coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin-like conformation that opens upon receptor binding. Variation of the coiled-coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real-time.
| Original language | English |
|---|---|
| Pages (from-to) | 17079-17083 |
| Number of pages | 5 |
| Journal | Angewandte Chemie. International Edition |
| Volume | 57 |
| Issue number | 52 |
| Early online date | 9 Nov 2018 |
| DOIs | |
| Publication status | Published - 21 Dec 2018 |
Funding
We are grateful to the group of Prof. H. Waldmann (MPI Dortmund) for access to the CD spectrometer and to the group of Prof. C. Czeslik (TU Dortmund) for their support and the access to DLS instrumentation. We thank the European Research Council (ERC; ERC starting grant, no. 678623) and we are grateful for support by AstraZeneca, Bayer CropScience, Bayer HealthCare, Boehringer Ingel-heim, Merck KGaA, and the Max Planck Society.
| Funders | Funder number |
|---|---|
| Boehringer Ingel-heim | |
| AstraZeneca | |
| Boehringer Ingelheim | |
| Bayer CropScience | |
| Merck KGaA | |
| Horizon 2020 Framework Programme | 678623 |
| European Research Council | |
| Bayer HealthCare | |
| Max-Planck-Gesellschaft |
Keywords
- conformational constraint
- heterodimeric coiled-coil
- molecular beacons
- molecular devices
- protein–protein interactions