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Dynamic Electrochemical Membranes for Continuous Affinity Protein Separation
A membrane system with nanometer‐scale thick electrodes is able to selectively bind genetically modified proteins and pump them across the membrane with sequential voltage pulses. The electrodes are located at the first 20 nm of pore entrances to specifically capture targeted proteins and block non‐...
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Published in: | Advanced functional materials 2014-07, Vol.24 (27), p.4317-4323 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | A membrane system with nanometer‐scale thick electrodes is able to selectively bind genetically modified proteins and pump them across the membrane with sequential voltage pulses. The electrodes are located at the first 20 nm of pore entrances to specifically capture targeted proteins and block non‐specific protein transport through the pores during the binding cycle. During the release cycle, concentration of imidazole is controlled to keep the pore blocked while releasing proteins at the bottom edge of the electrode. A separation factor for GFP:BSA of 16 was achieved with observed GFP electrophoretic mobility of 2.54 × 10−6 cm2 V−1 s−1. This non‐optimized system with a membrane area of 0.75 cm2 has the same throughput as 1 mL of commercially available chromatography columns showing viability as a continuous process. This system will enable continuous separation of expressed proteins directly from fermentation broths dramatically simplifying the separation process as well as reducing bio‐pharmaceutical production costs.
A dynamic electrochemical membrane system with nanometer‐scale thick electrodes, mimicking the function of cell wall transporters, is reported for continuous affinity protein separation. The system is able to actively capture the affinity protein onto the pore entrance to block other proteins in a sequential/hopping manner, allowing selective transport. |
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ISSN: | 1616-301X 1616-3028 |
DOI: | 10.1002/adfm.201303707 |