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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kreir, Mohamed Fertig, Niels Dondapati, Srujan Kumar Wüstenhagen, Doreen A. Kubick, Stefan Brüggemann, Andrea Quast, Robert B. |
| Description | Country affiliation: Germany Author Affiliation: Dondapati SK ( Fraunhofer Institute for Biomedical Engineering, Branch Potsdam-Golm, Am Mühlenberg 13, 14476 Potsdam, Germany.); Kreir M ( Nanion Technologies GmbH, Gabrielenstr. 9, 80636 Munich, Germany.); Quast RB ( Fraunhofer Institute for Biomedical Engineering, Branch Potsdam-Golm, Am Mühlenberg 13, 14476 Potsdam, Germany.); Wüstenhagen DA ( Fraunhofer Institute for Biomedical Engineering, Branch Potsdam-Golm, Am Mühlenberg 13, 14476 Potsdam, Germany.); Brüggemann A ( Nanion Technologies GmbH, Gabrielenstr. 9, 80636 Munich, Germany.); Fertig N ( Nanion Technologies GmbH, Gabrielenstr. 9, 80636 Munich, Germany.); Kubick S ( Fraunhofer Institute for Biomedical Engineering, Branch Potsdam-Golm, Am Mühlenberg 13, 14476 Potsdam, Germany. Electronic address: stefan.kubick@ibmt.fraunhofer.de.) |
| Abstract | The potassium channel KcsA was heterologously expressed in a eukaryotic cell-free system. Both, the expression yields and functional analysis of the protein were reported. Qualitative and quantitative analyses of KcsA expression were performed by using (14)C-labeled leucine as one of the amino acids supplemented in the cell-free reaction mixture. There was a time dependent increase in the protein yield as well as the intensity of the native tetramer band in insect cell derived microsomes. Electrophysiology measurements demonstrated the functional activity of the microsomes harboring KcsA showing single-channel currents with the typical biophysical characteristics of the ion channel. The channel behavior was asymmetric and showed positive rectification with larger currents towards positive voltages. KcsA channel currents were effectively blocked by potassium selective barium (Ba(2+)). This functional demonstration of an ion channel in eukaryotic cell-free system has a large potential for future applications including drug screening, diagnostic applications and functional assessment of complex membrane proteins like GPCRs by coupling them to ion channels in cell-free systems. Furthermore, membrane proteins can be expressed directly from linear DNA templates within 90 min, eliminating the need for additional cloning steps, which makes this cell-free system fast and efficient. |
| ISSN | 09565663 |
| Volume Number | 59 |
| e-ISSN | 18734235 |
| Journal | Biosensors and Bioelectronics |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-09-15 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Bacterial Proteins Metabolism Potassium Channels, Voltage-gated Streptomyces Lividans Animals Chemistry Genetics Cell Line Cloning, Molecular Microsomes Protein Biosynthesis Protein Multimerization Journal Article Research Support, Non-u.s. Gov't Discipline Biotechnology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Nanoscience and Nanotechnology Medicine Biophysics Biomedical Engineering Biotechnology Electrochemistry |
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