Aquafoldmer-Based Aquaporin-like Synthetic Water Channel
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Synthetic water channels were developed with an aim to replace aquaporins for possible uses in water purification, while concurrently retaining aquaporins' ability to conduct highly selective superfast water transport. Among the currently available synthetic water channel systems, none possesses water transport properties that parallel those of aquaporins. In this report, we present the first synthetic water channel system with intriguing aquaproin-like features. Employing a "sticky end"-mediated molecular strategy for constructing abiotic water channels, we demonstrate that a 20% enlargement in angstrom-scale pore volume could effect a remarkable enhancement in macroscopic water transport profile by 15 folds. This gives rise to a powerful synthetic water channel able to transport water at a speed of ∼3 × 109 H2O s-1 channel-1 with a high rejection of NaCl and KCl. This high water permeability, which is about 50% of aquaporin Z's capacity, makes channel 1 the fastest among the existing synthetic water channels with high selectivity.Cell permeability
Homeostasis
Aquaporin 1
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Synthetic water channels were developed with an aim to replace aquaporins for possible uses in water purification, while concurrently retaining aquaporins' ability to conduct highly selective superfast water transport. Among the currently available synthetic water channel systems, none possesses water transport properties that parallel those of aquaporins. In this report, we present the first synthetic water channel system with intriguing aquaproin-like features. Employing a "sticky end"-mediated molecular strategy for constructing abiotic water channels, we demonstrate that a 20% enlargement in angstrom-scale pore volume could effect a remarkable enhancement in macroscopic water transport profile by 15 folds. This gives rise to a powerful synthetic water channel able to transport water at a speed of ∼3 × 109 H2O s-1 channel-1 with a high rejection of NaCl and KCl. This high water permeability, which is about 50% of aquaporin Z's capacity, makes channel 1 the fastest among the existing synthetic water channels with high selectivity.
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The cloning and molecular characterization of water channels, generically called aquaporins, have marked a pivotal point in our understanding of water movements across epithelial barriers. Nevertheless, the mechanisms underlying water transfer across these barriers at the molecular and cellular level are not yet clarified. We analyze here the role of the different driving forces moving water across epithelia and the biophysical properties of the water channels. We will also review the recently cloned epithelial members of the aquaporin family, including their expression and distribution in different tissues.
Water transfer
Cloning (programming)
Aquaporin 1
Water Transport
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A family of structurally similar channel-forming membrane glycoproteins, termed water channels or aquaporins, accounts for the constitutive as well as vasopressin-regulated water permeability in respective epithelia. Heterogeneity of aquaporins provides a molecular basis for some genetic diseases and treatment of certain diseases with disturbances in water homeostasis.
Aquaporin 2
Homeostasis
Water Transport
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Aquaporins are integral membrane proteins, which function as specialized water channels to facilitate the passage of water through the cell membrane. In mammals six different aquaporins have been identified up to now, four of which (aquaporin-1 to aquaporin-4) are expressed in the kidney. Because of its importance for normal water homeostasis and its involvement in many water balance disorders, aquaporin-2, the predominant vasopressin-regulated water channel of the renal collecting duct, is discussed in detail.
Aquaporin 2
Aquaporin 1
Homeostasis
Water Transport
Aquaporin 3
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Aquaporin 1
Water Transport
Aquaporin 4
Aquaporin 2
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Aquaporin 2
Aquaporin 1
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The aquaporin water channels are expressed in various fluid-transporting epithelia. Physiological and genetic investigations have revealed that aquaporin channel-like intrinsic protein is expressed in numerous tissues, but its significance in water transport physiology is unclear. It has been shown that aquaporin-collecting duct is a vasopressin-responsive water channel, and that it is regulated by a membrane shuttle mechanism. Three unique models for a water pore have been presented but further studies will be required to verify them. New aquaporin members have been isolated and their discrete localization may reflect their specific physiological roles.
Aquaporin 2
Water Transport
Aquaporin 3
Aquaporin 1
Water metabolism
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Aquaporin 1
Aquaporin 2
Water Transport
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Artificial aquaporins are synthetic molecules that mimic the structure and function of natural aquaporins (AQPs) in cell membranes. The development of artificial aquaporins would provide an alternative strategy for treatment of AQP-related diseases. In this report, an artificial aquaporin has been constructed from an amino-terminated tubular molecule, which operates in a unimolecular mechanism. The artificial channel can work in cell membranes with high water permeability and selectivity rivaling those of AQPs. Importantly, the channel can restore wound healing of the cells that contain function-lost AQPs.
Cell permeability
Aquaporin 1
Cell membrane
Water Transport
Membrane permeability
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