AsianScientist (Aug. 23, 2018) – Scientists in Singapore have developed a family of pore-forming monopeptides made from a single type of amino acid. Their work is published in the Journal of the American Chemical Society.
Pore-forming peptides form channels through cellular membranes for the transportation of ions such as chlorides and iodides in and out of a cell. The formation of these channels is crucial for the precise regulation of our bodies’ physiological processes, cellular defenses and immune responses. For example, patients with cystic fibrosis suffer from a defective gene that reduces the transport of such ions, thus dehydrating the mucus layer in the lungs. This results in a build-up of thick and viscous mucus that causes breathing difficulties.
Hence, designing artificial ion channels is an area of increasing interest, particularly channels that can self-assemble in a controlled manner from simple molecular precursors. Many current systems utilize complex, high molecular weight components, which greatly limit their potential for future therapeutic applications.
In the present study, scientists at the Institute of Bioengineering and Nanotechnology (IBN) of the Agency for Science, Technology and Research (A*STAR) in Singapore focused on developing artificial pore-forming monopeptides based on a single amino acid. They were able to create synthetic ion channels with pore sizes smaller than 1.0 nm in diameter. These channels could transport negatively-charged ions, including chloride, efficiently across the membrane.
The researchers noted that their approach presents opportunities to design novel, small molecule-based artificial ion channels which could result in better therapies for ion channel dysfunction. Such channels could also be used as anti-bacterial or anti-cancer agents.
“The IBN research team originally studied ion-transporting molecules designed to function as gelators to coalesce oil spills in water. Through this, they discovered that one of the gelators was of significant toxicity, causing them to explore whether the molecule might self-assemble into a pore-like structure in the cell membrane and cause an imbalance of ions. This hypothesis turned out to be true and led to a completely new principle of the molecular design of ion channels,” said Dr. Ichiro Hirao, covering executive director of IBN.
The article can be found at: Ren et al. (2018) Pore-Forming Monopeptides as Exceptionally Active Anion Channels.
Source: A*STAR; Photo: Shutterstock.
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