A new artificial skin from Switzerland is soft, sensitive and stretchy, an Australian lab is developing a patch that could grow replacement heart tissue, and researchers in the U.K. are using a rare and ancient element to kill tumors. Scientists are casting their nets far and wide in this week’s coolest discoveries.
What is it? A new soft artificial skin, made of silicone and electrodes and developed by scientists at Switzerland’s École Polytechnique Fédérale de Lausanne, replicates haptic feedback — that is, the sense of touch — and can adapt to the movements of whoever is wearing it.
Why does it matter? Soft, sensitive artificial skin could be used for medical rehabilitation, as well as in human-computer interfaces like augmented and virtual reality. “This is the first time we have developed an entirely soft artificial skin where both sensors and actuators are integrated,” said Harshal Sonar, lead author of a study in Soft Robotics. “This gives us closed-loop control, which means we can accurately and reliably modulate the vibratory stimulation felt by the user. This is ideal for wearable applications, such as for testing a patient’s proprioception in medical applications.” (“Proprioception” = the sense of the body and its position and movement in space. It’s sometimes called the sixth sense.)
How does it work? The skin is made of layers of different tech, including an inflatable membrane layer and actuators tuned to different pressures and frequencies. Electrodes in a sensor on top of the membrane, according to EPFL, “measure the skin’s deformation continuously and send the data to a microcontroller, which uses this feedback to fine-tune the sensation transmitted to the wearer in response to the wearer’s movements and changes in external factors.” The material is also stretchable, which makes it particularly useful in the real world.
What is it? Scientists at Australia’s University of New South Wales have found a way to use silk as a kind of scaffolding that could form patches to help repair damaged heart tissue.
Why does it matter? “The idea behind the patch is essentially to replace the bit of the heart that has died with a living tissue that we’ve grown in the lab,” Dr. Jelena Rnjak-Kovacina told the Daily Telegraph. Silk is a promising biomaterial to use in such patches. Researchers want to attach heart stem cells to the silk scaffolding and let them grow, but they need to be able to control the direction of their growth — to make sure they resemble actual heart tissue. The UNSW work attempts to do this with some new materials and techniques: namely, 3D-printed silicon molds and freezing temperatures.
How does it work? Habib Joukhdar, a Ph.D. student in Rnjak-Kovacina’s lab, filled those molds with silk and water, when placed them on a copper plate cooled by dry ice, which caused the mixture to freeze in a single direction — from one end to the other. The structure of the ice crystals, it turned out, closely resembled the micro-level structure of heart muscle. Joukhdar explained: “Silk is a protein. As the ice begins to grow through the silk solution, this protein gathers around the growing ice. As the ice moves upwards, it pushes this protein out of the way. Then when it’s completely frozen, you can freeze-dry it, and that removes the ice. So you end up with pores that are a negative cast in the silk of what used to be the ice.” Developing the scaffolding itself is a big step, but Rnjak-Kovacina told the Daily Telegraph it’s just an initial one — translating the findings into clinical practice could take a decade.
What is it? Iridium, an element linked to the meteorite that killed the dinosaurs, could also be effective in killing cancer, according to a new collaboration led by scientists at the U.K.’s University of Warwick.
Why does it matter? The treatment may be particularly well-suited to bladder, lung, esophageal, brain and skin cancers, according to a press release. Warwick’s Peter Sadler said: “There is an increasing interest in reducing the side effects of cancer treatment as much as possible and anything that can be selective in what it targets will help with that. The compound that we have developed would not be very toxic at all, we would give it to the cancer cells, allow a little time for it to be taken up, then we would irradiate it with light and activate it in those cells. We would expect killing of those cancer cells to occur very quickly compared with current methods.”
How does it work? By way of photodynamic therapy, a form of cancer treatment in which doctors inject patients with a photosensitizing agent that, when activated by a certain wavelength of light, kills cancer cells. Most current methods depend on the presence of oxygen, though, whereas many tumors are hypoxic — that is, low in oxygen. But with iridium — an extremely rare element whose presence in subterranean sediment layers (by the way) helped support the asteroid-extinction hypothesis — the treatment can work at even low oxygen concentrations. Once activated by light, the iridium compound attacks the “energy-producing machinery in the cancer cells,” according to the university. The findings are explained further in Nature Chemistry.
What is it? Researchers at the Massachusetts Institute of Technology and the Broad Institute have come up with a new way to quickly image synaptic proteins — crucial links in the brain’s wiring.
Why does it matter? Synapses are the “connections that transmit messages from neuron to neuron,” according to MIT, and the brain has trillions of them, made of hundreds of different proteins. Malfunctioning synapses can lead to autism, schizophrenia and Alzheimer’s disease, and new treatments for those conditions could arise from better ways to examine and catalog the synaptic proteins. MIT biological engineering professor Mark Bathe: “Multiplexed imaging is important because there’s so much variability between synapses and cells, even within the same brain. You really need to look simultaneously at proteins in the sample to understand what subpopulations of different synapses look like, discover new types of synapses, and understand how genetic variations impact them.”
How does it work? The researchers built off an existing imaging method called DNA PAINT, in which proteins and other molecules are labeled with a DNA-antibody probe, then imaged after being bound with a fluorescent DNA molecule. The imaging of each individual protein takes a long time with this method, though, and the MIT and Harvard team found a way to — long story short; the process is described in Nature Communications — speed it up. They used their technique to label 12 different synaptic proteins, including one “scaffolding protein” that’s been linked to both autism and schizophrenia.
What is it? Speaking of fluorescence: Researchers at the California Institute of Technology developed a method to use it, along with ultrasound, to get a closer look at how cells work deep in the body.
Why does it matter? Their new technique is an extension of an existing method of studying cells that relies on pieces of DNA called reporter genes, explains Caltech: “One particularly popular reporter gene encodes something called the green fluorescent protein (GFP), which, true to its name, is a protein that glows bright green. So, if a researcher wants to learn more about how cells become neurons, they can insert the GFP gene alongside a neuronal gene into an embryo’s DNA.” One limitation of this is that light can’t penetrate well through living tissue, so researchers haven’t been able to use it to peer deep inside an organism.
How does it work? Enter ultrasound — which can see deeply through tissue. The Caltech researchers developed something they called “acoustic reporter genes,” which contain proteins with tiny air-filled compartments in them — which are visible in ultrasound imaging. Those proteins come from bacteria, though, so first researchers had to figure out how to make the bacterial DNA intelligible to the mammalian cells it was being inserted into. It’s been a long process, said Caltech professor Mikhail Shapiro: “There has been more than 20 years of work improving fluorescent proteins, and we probably have 20 years of work to improve what we’ve developed, but this is a key proof of concept.” The findings are published in Science.