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Aquaporins

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.

Facilitated Transport

Facilitated Transport

The chemical and physical properties of plasma membranes cause them to be selectively permeable. Since plasma membranes have both hydrophobic and hydrophilic regions, substances need to be able to transverse both regions. The hydrophobic area of membranes repels substances such as charged ions. Therefore, such substances need special membrane proteins to cross a membrane successfully. In facilitated transport, also known as facilitated diffusion, molecules and ions travel across a...

Facilitated Transport

Facilitated Transport

The chemical and physical properties of plasma membranes cause them to be selectively permeable. Since plasma membranes have both hydrophobic and hydrophilic regions, substances need to be able to transverse both regions. The hydrophobic area of membranes repels substances such as charged ions. Therefore, such substances need special membrane proteins to cross a membrane successfully. In facilitated transport, also known as facilitated diffusion, molecules and ions travel across a...

Pore Transport and Ion-Pair Transport

Pore Transport and Ion-Pair Transport

Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...

Multi-pass Transmembrane Proteins and β-barrels

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...

The Significance of Membrane Transport

The Significance of Membrane Transport

The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...

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Related Experiment Video

Updated: Nov 5, 2025

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Foldamer-based ultrapermeable and highly selective artificial water channels that exclude protons.

Arundhati Roy^1,2, Jie Shen¹, Himanshu Joshi³

¹Department of Chemistry, College of Science, Hainan University, Haikou, Hainan, China.

Nature Nanotechnology

|May 21, 2021

Summary

Researchers developed artificial water channels (AWCs) that mimic aquaporins (AQPs). These novel AWCs demonstrate superior water transport and selectivity, even excluding protons, outperforming natural AQPs.

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Last Updated: Nov 5, 2025

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Published on: June 28, 2019

Area of Science:

Biomimetic materials science
Supramolecular chemistry
Membrane technology

Background:

Aquaporins (AQPs) facilitate rapid, selective water transport but struggle with proton exclusion.
Artificial water channels (AWCs) inspired by AQPs show promise for water purification and desalination.
Replicating the proton-excluding capability of AQPs in AWCs remains a significant challenge.

Purpose of the Study:

To design and synthesize novel biomimetic artificial water channels (AWCs) that surpass aquaporin (AQP) performance.
To achieve high water transport rates while maintaining selectivity against monovalent ions and protons.
To explore the potential of polymeric foldamers as building blocks for advanced water-conducting channels.

Main Methods:

Development of helically folded, pore-forming polymeric foldamers.
Modular tuning of the interior pore surface hydrophobicity.
Characterization of water and ion transport properties of the synthesized AWCs.
Comparative performance analysis against natural aquaporins (e.g., AQP1).

Main Results:

The novel AWCs exhibit water transport rates 2.5 times higher than AQP1.
Achieved high water-over-monovalent-ion selectivity, approximately 10^8.
Demonstrated effective rejection of salts (NaCl, KCl) and protons.
The performance surpasses that of natural AQPs in terms of water transport and selectivity.

Conclusions:

The developed polymeric foldamer-based AWCs represent a significant advancement in artificial water channel technology.
These AWCs offer superior water transport and selectivity compared to natural AQPs, including proton exclusion.
The findings open new avenues for highly efficient desalination, water purification, and other separation applications.