Abstract
In recent years, the use of biomimetic membranes that incorporate membrane proteins, i.e., biomimetic-hybrid membranes, has increased almost exponentially. Key membrane proteins in these systems have been aquaporins, which selectively permeabilize cellular membranes to water. Aquaporins may be incorporated into synthetic lipid bilayers or to more stable structures made of block copolymers or solid-state nanopores. However, translocation of aquaporins to these alien environments has adverse consequences in terms of performance and stability. Aquaporins incorporated in biomimetic membranes for use in water purification and desalination should also withstand the harsh environment that may prevail in these conditions, such as high pressure, and presence of salt or other chemicals. In this respect, modified aquaporins that can be adapted to these new environments should be developed. Another challenge is that biomimetic membranes that incorporate high densities of aquaporin should be defect-free, and this can only be efficiently ascertained with the availability of completely inactive mutants that behave otherwise like the wild type aquaporin, or with effective non-toxic water channel inhibitors that are so far inexistent. In this review, we describe approaches that can potentially be used to overcome these challenges.
Highlights
In recent years, the use of biomimetic membranes that incorporate membrane proteins, i.e., biomimetic-hybrid membranes, has increased almost exponentially
Many challenges must be overcome before the use of aquaporin-based biomimetic membranes can be considered mainstream
Apart from constructing biomimetic membranes based on traditionally used E. coli AqpZ, other aquaporin isoforms may be tested for higher permeability and/or better insertion efficiency in
Summary
Aquaporins (AQPs) are integral membrane proteins that transport water through cellular membranes [1,2,3]. A target AQP encoded by a host expression vector will be expressed in fusion with an affinity tag, commonly a polyhistidine (6His) tag Once this recombinant AQP is produced from host cells, host lysis is closely followed by reconstitution of the recombinant AQP from host cell membranes into stabilizing biomimetic environments, i.e., detergent micelles. High production of AQP proteins is possible using cell- free (CF) expression system, a novel approach which mimics the natural cell cytoplasmic environment for protein synthesis This holds advantages over traditional in vivo membrane protein expression in living cells, such as elimination of toxicity to host cell physiology due to membrane incorporation of recombinant proteins, and overloading of essential cellular protein-targeting machineries in order to overexpress a foreign protein [29]. By introducing isotopically- labelled or fluorescence-enhanced amino acids into the reaction mixture, efficient labelling of the target AQP is possible
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