Highly permeable biomimetic reverse osmosis membrane with amphiphilic peptide stabilized aquaporin as water filtering agent. Issue 15 (27th December 2017)

• Record Type: Journal Article
• Authors: He, Yuan; Hoi, Hiofan; Abraham, Sinoj; Montemagno, Carlo D.
• Is Part Of: Journal of applied polymer science. Volume 135:Issue 15(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-12-27
• Subjects: biodegradable -- biomaterials -- biopolymers and renewable polymers -- biosynthesis of polymers -- proteins; Polymers -- Periodicals; Polymerization -- Periodicals; 668.9
• DOI: 10.1002/app.46169
• Languages: English
• ISSNs: 0021-8995

Abstract

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. Abstract :