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Aquaporins (AQPs) are naturally occurring water channel proteins. They can facilitate water molecule translocation across cellular membranes with exceptional selectivity and high permeability that are unmatched in synthetic membrane systems. These unique properties of AQPs have led to their use as functional elements in membranes in recent years. However, the intricate nature of AQPs and concerns regarding their stability and processability have encouraged researchers to develop synthetic channels that mimic the structure and properties of AQPs and other biological water-conducting channels. These channels have been termed artificial water channels. This article reviews current progress and provides a historical perspective as well as an outlook toward developing scalable membranes based on artificial water channels.
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Download all Supplemental Material as a single PDF. Includes Supplemental Text, and Supplemental Figures 1-2 (also reproduced below).
Supplemental Figure 1. Chemical synthesis routes of representative self-assembling water channels, including (a) azole based channels, (b) triarylamine channels and (d) foldamers.
Supplemental Figure 2. Chemical synthesis routes for pillar[5]arene based unimolecular water channels. This synthesis strategy can be summarized as two steps. First step is to activate pillar[5]arene’s hydroxyl groups into desirable reactive linkers. Second step is to extend side chains on these linkers. In the process of chain extension, the chain monomers can be introduced step by step to achieve extended tubular structure as shown in case of HAP synthesis. Otherwise, pre-elongated chains (NH2-D-Phe-L-Phe-D-Phe-COOMe) can be introduced as shown in PAP[5] synthesis route.