Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-017-11723-x
Title: Quantification of Aquaporin-Z reconstituted into vesicles for biomimetic membrane fabrication
Authors: Gan H.X. 
Zhou H.
Lin Q. 
Tong Y.W. 
Keywords: aquaporin
gold
metal nanoparticle
biomimetics
cell membrane
chemistry
metabolism
permeability
procedures
transmission electron microscopy
ultracentrifugation
ultrastructure
Aquaporins
Biomimetics
Cell Membrane
Gold
Metal Nanoparticles
Microscopy, Electron, Transmission
Permeability
Ultracentrifugation
Issue Date: 2017
Citation: Gan H.X., Zhou H., Lin Q., Tong Y.W. (2017). Quantification of Aquaporin-Z reconstituted into vesicles for biomimetic membrane fabrication. Scientific Reports 7 (1) : 11565. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-017-11723-x
Abstract: Aquaporin incorporated biomimetic membranes are anticipated to offer unprecedented desalination capabilities. However, the lack of accurate methods to quantify the reconstituted aquaporin presents a huge hurdle in investigating aquaporin performance and optimizing membrane fabrication. Herein, we present three quantification methods to determine the Aquaporin-Z reconstituted into E. coli lipid vesicles: 1) nanogold labeling with transmission electron microscopy (TEM) visualization, 2) nickel labeling with inductively coupled plasma-mass spectrometry (ICP-MS) and 3) gel electrophoresis. The TEM method serves as a quick way to determine if aquaporin has been reconstituted, but is not quantitative. The numerical results from quantitative methods, ICP-MS and gel electrophoresis, correlate closely, showing that 60 ± 20% vs 66 ± 4% of Aquaporin-Z added is successfully reconstituted into vesicles respectively. These methods allow more accurate determination of Aquaporin-Z reconstituted and loss during reconstitution, with relatively commonly available equipment and without complex sample handling, or lengthy data analysis. These would allow them to be widely applicable to scientific studies of protein function in the biomimetic environment and engineering studies on biomimetic membrane fabrication. © 2017 The Author(s).
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/175167
ISSN: 20452322
DOI: 10.1038/s41598-017-11723-x
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