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Highly permeable biomimetic reverse osmosis membrane with amphiphilic peptide stabilized aquaporin as water filtering agent
Author(s) -
He Yuan,
Hoi Hiofan,
Abraham Sinoj,
Montemagno Carlo D.
Publication year - 2018
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.46169
Subject(s) - aquaporin , membrane , amphiphile , desalination , reverse osmosis , water transport , materials science , aqueous solution , chemical engineering , circular dichroism , chemistry , biophysics , biology , biochemistry , polymer , engineering , environmental engineering , water flow , organic chemistry , copolymer
ABSTRACT The shortage of fresh water is one of the most critical problems our society must address. The most commonly accepted method to produce fresh water is by membrane systems. Since the discovery of aquaporins (AQPs) (water channel proteins), researchers have been trying to incorporate them as functional units in biomimetic membranes to achieve superior water permeability and solute rejection. However, it still remains challenging due to the lack of an effective strategy to stabilize AQPs and fabricate robust membranes. Here, we report the utilization of an amphiphilic peptide (BP1) to stabilize AQPs and use the resulting protein–BP1 complex for desalination purposes. We demonstrated the secondary structure and stability of protein–BP1 complex in aqueous solution using circular dichroism and transmission electron microscopy. The resulting membrane with aquaporin incorporation showed water permeability of 12.33 LMH, improved 28% compared to mutant control membrane, and 83.6% compared to traditional polyamide membrane, while maintaining the high sale rejection (96%). These results demonstrate a great potential of this new incorporating technique for desalination applications. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018 , 135 , 46169.