Natural water channels, aquaporins are transmembrane proteins which are highly selective for water molecules. Their unique structure featuring a narrow inner pore allows single file of water molecules to cross across the membrane with the transport rate of 109 water molecules/second. Aquaporin-embedded biomimetic membranes have been developed for water purification. They are energy efficient, but producing sufficient quantity of the bulky protein is expensive.

In an effort to improve on this, we have designed artificial channels (foldamer) based on information from the aquaporin structure. These foldamers are helical oligourea-based synthetic polymers, which have self-assembling properties and are designed to form controllable water-filled polar channels through sequence manipulation.

Preliminary studies have shown that these foldamer pores transport water. Because of their chemistry, foldamers are non-biodegradable, stable polymers and hence should offer longer life span for fabricated membranes. These novel foldamers have the potential to be covalently attached to synthetic membrane matrices. We propose to further design efficient foldamers with selective water and ion transport properties.