Abstract

The permeability and solute transport characteristics of amphiphilic triblock-polymer vesicles containing the bacterial water-channel protein Aquaporin Z (AqpZ) were investigated. The vesicles were made of a block copolymer with symmetric poly-(2-methyloxazoline)-poly-(dimethylsiloxane)-poly-(2-methyloxazoline) (PMOXA 15 -PDMS 110 -PMOXA 15 ) repeat units. Light-scattering measurements on pure polymer vesicles subject to an outwardly directed salt gradient in a stopped-flow apparatus indicated that the polymer vesicles were highly impermeable. However, a large enhancement in water productivity (permeability per unit driving force) of up to ≈800 times that of pure polymer was observed when AqpZ was incorporated. The activation energy ( E a ) of water transport for the protein-polymer vesicles (3.4 kcal/mol) corresponded to that reported for water-channel-mediated water transport in lipid membranes. The solute reflection coefficients of glucose, glycerol, salt, and urea were also calculated, and indicated that these solutes are completely rejected. The productivity of AqpZ-incorporated polymer membranes was at least an order of magnitude larger than values for existing salt-rejecting polymeric membranes. The approach followed here may lead to more productive and sustainable water treatment membranes, whereas the variable levels of permeability obtained with different concentrations of AqpZ may provide a key property for drug delivery applications.

Keywords

MembraneVesicleAquaporinPolymerWater transportSynthetic membraneChemistryPermeability (electromagnetism)AmphiphilePermeationChemical engineeringSemipermeable membraneBiophysicsCopolymerChromatographyPolymer chemistryWater flowOrganic chemistryBiochemistryBiology

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Year
2007
Type
article
Volume
104
Issue
52
Pages
20719-20724
Citations
694
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Manish Kumar, Mariusz Grzelakowski, Julie L. Zilles et al. (2007). Highly permeable polymeric membranes based on the incorporation of the functional water channel protein Aquaporin Z. Proceedings of the National Academy of Sciences , 104 (52) , 20719-20724. https://doi.org/10.1073/pnas.0708762104

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DOI
10.1073/pnas.0708762104