Researchers have been growing mini organs in the lab to understand the effects of the new coronavirus on the body, the anti-COVID-19 drug remdesivir is being tested in inhaler form, and a collaboration of chemists from Germany and Tennessee found a better way to produce a superthin, superstrong supermaterial. Read on for more of the week’s supercool scientific findings.
What is it? Teams of scientists around the world have been using lab-grown organoids — mini organs — to better understand how the SARS-CoV-2 virus attacks the body.
Why does it matter? Even with the eyes of many of the world’s scientists trained on it for months, much about the workings of SARS-CoV-2 — the coronavirus that causes COVID-19 — remains mysterious. One question, for instance, is whether organ damage seen in the bodies of COVID patients is caused by the virus itself, or by some kind of secondary infection. Virologists, according to a new article in Nature, “typically study viruses using cell lines or animal cells cultured in a dish,” which offers only a limited view of a virus’ effects. “The beauty of organoids is that they resemble the true morphology of tissues,” said Thomas Efferth, a cell biologist at Germany’s Johannes Gutenberg University.
How does it work? Different teams have used organoids to focus on different areas. Some, for instance, have shed light into how the virus initially infects the respiratory system. In Barcelona, Núria Montserrat and colleagues used organoids to demonstrate how the virus travels between organs: As Nature described the findings, “SARS-CoV-2 can infect the endothelium — the cells lining the blood vessels — which then allows viral particles to leak out into the blood and circulate around the body.” Organoids could also be used as a kind of test bed for possible COVID-fighting drugs.
What is it? The biopharmaceutical company Gilead announced this week that it received approval from the Food and Drug Administration to begin Phase I clinical trials of an inhaled version of remdesivir, the first antiviral drug to show promise against COVID-19.
Why does it matter? The FDA issued an Emergency Use Authorization for remdesivir in May, but currently it’s only being administered intravenously to hospital patients. In an open letter, CEO Daniel O’Day said Gilead is entering “the next wave of clinical development,” by testing different delivery methods for remdesivir as well as its use in combination with other therapies, like anti-inflammatory medicines.
How does it work? Though the drug is currently being given to patients hospitalized with COVID-19, if it were able to be administered through a nebulizer — which turns liquid medicines into mist — the idea is that patients could take it at earlier stages of infection, helping to slow the virus’ spread through the body. “If you could get rid of the virus before they develop those disease symptoms, you would probably have better clinical outcomes across many patients,” Columbia University virologist Angela Rasmussen told the New York Times.
What is it? A startup called Macro-eyes developed an artificial intelligence tool that was able to reduce vaccine wastage by 96% in parts of Tanzania — and, more broadly, wants to use AI to help hospitals better manage patient care.
Why does it matter? Though more children than ever are getting vaccinated against preventable diseases, there are still some logistical hitches for health authorities — such as not knowing who will show up for vaccinations at the clinic. That can lead to shortages, if many people come at once, or surpluses that need to be discarded. The vaccine-prediction tool, called Connected Health AI Network, builds off a previous product created by the company: the patient-scheduling platform Sibyl, which has reduced wait times at one busy heart hospital by more than 75%.
How does it work? CEO Benjamin Fels, a former hedge fund trader, founded Macro-eyes with Suvrit Sra, a professor at the Massachusetts Institute of Technology, and the pair began developing algorithms in 2013 to help medical centers, including Stanford School of Medicine, develop better treatment plans. “There are themes we established at Stanford that remain today,” Fels told MIT News, such as making sure humans are “in the loop. We’re not just learning from the data, we’re also learning from the experts. The other is multidimensionality. We’re not just looking at one type of data; we’re looking at 10 or 15 types, [including] images, time series, information about medication, dosage, financial information, how much it costs the patient or hospital.”
What is it? By running computer models of protein interactions, researchers from MIT Media Lab and the Center for Bits and Atoms have come up with a possible way to prevent the new coronavirus from replicating itself within cells.
Why does it matter? As the pandemic has spread, researchers have turned to computers to model the interactions of potential COVID-fighting compounds, and they’ve also searched for ways to block the coronavirus’ infamous spike protein from infecting human cells. This research continues in both those veins, focusing on small protein fragments called peptides. Pranam Chatterjee, the lead author of a new paper that’s been published on the preprint server bioRxiv — but hasn’t yet undergone peer review — said, “Our idea was to use computational techniques to engineer a peptide that could be a therapeutic for COVID-19. Once the peptide gets in the cell, it can simply tag and degrade the virus.”
How does it work? The researchers began with the human protein ACE2, which binds to the coronavirus’ spike protein; then they modeled different ways to break it down into peptide fragments, and simulated how each of about 25 candidate peptides would interact with — and degrade — a fragment of the spike protein called the receptor-binding domain, or RBD. They eventually developed a “mutant peptide that improved the degradation rate to over 50%,” according to MIT News. Having achieved promising results in human cells, the team plans more cell and animal studies.
What is it? A team of chemists from Germany’s Martin-Luther-Universität (MLU) Halle-Wittenberg, the University of Tennessee and Oak Ridge National Laboratory have found a better way to produce graphene nanoribbons.
Why does it matter? Thin, strong and versatile, graphene — a single layer of carbon atoms in a honeycomb pattern — has been heavily hyped as a supermaterial, of interest to the electrical and computer industries as a semiconductor, along with a host of other applications. As a pair of scientists explained to The Verge in 2018, one atom-thick sheet of graphene could bear the weight of an elephant — but the material is hard to produce due to technical challenges.
How does it work? The ribbons that the German and Tennessee teams produced had previously been synthesized on gold surfaces, in a process that was “not only comparatively expensive, but also impractical,” said MLU’s Konstantin Amsharov. The team instead found a way to synthesize the nanoribbons, for the first time, on the surface of titanium oxide. Amsharov said, “Our new method allows us to have complete control over how the graphene nanoribbons are assembled. The process is technologically relevant as it could also be used at an industrial level. It is also more cost-effective than previous processes.”