Category: 7. Science

New computer simulations that model every atom of a protein as it folds into its final three-dimensional form support the existence of a recently identified type of protein misfolding. Proteins must fold into precise three-dimensional shapes – called their native state – to carry out their biological functions. When proteins misfold, they can lose function and, in some cases, contribute to disease. The newly spotted misfolding results in a change to a protein’s structure – either a loop that traps another section of the protein forms when it shouldn’t or doesn’t when it should – that disrupts its function and can persist in cells by evading the cell’s quality control system. The simulated misfolds also align closely with structural changes inferred from experiments that track protein folding using mass spectrometry, according to the team led by researchers at Penn State.

“Protein misfolding can cause disease, including Alzheimer’s and Parkinson’s, and is thought to be one of the many factors that influence aging,” said Ed O’Brien, professor of chemistry in the Eberly College of Science, a co-hire of the Institute for Computational and Data Sciences at Penn State and the leader of the research team. “This research represents another step forward in our attempt to document and understand the mechanisms of protein misfolding. Our aim is to translate these fundamental discoveries into therapeutic targets that could help mitigate the impacts of these disorders and even aging.”

A paper describing the research appeared today (Aug. 8) in the journal Science Advances.

Proteins are composed of long strings of units called amino acids. A protein’s function relies on the sequence of those amino acids along the string, which determines how the string will fold into a three-dimensional structure. Sections of the protein can fold into helices, loops, sheets and various other structures which allows them to interact with other molecules and perform their functions. Any mistake during this folding process can disrupt these functions.

The new class of misfolding, recently identified by the O’Brien Lab, involves a change in entanglement status in the protein’s structure. Entanglement refers to sections of the string of amino acids looping around each other like a lasso or a knot. Sometimes an entanglement can form when it shouldn’t be there and sometimes an entanglement that is part of the protein’s native structure doesn’t form when it should.

“In our previous study, we used a coarser-grained simulation that only modeled the protein at the amino acid level not the atomic level,” said Quyen Vu, first author of the paper and a postdoctoral researcher in chemistry at Penn State who started the research as a graduate student at the Polish Academy of Sciences. “But there was concern in the community that such a model might not be realistic enough, as the chemical properties and bonding of the atoms that make up amino acids influence the folding process. So, we wanted to make sure we still saw this class of entanglement misfolding with higher-resolution simulations.”

The team first used all-atom models of two small proteins and simulated their folding. They found that both small proteins could form the misfolds just like in their coarser-grained simulations. However, unlike in their previous simulations, which modeled normal-sized proteins, the misfolds in these small proteins lasted only a short time. 

“We think that the misfolds in our previous simulations persisted for two main reasons,” Vu said. “First, to fix the misfold required backtracking and unfolding several steps to correct to entanglement status, and second, the misfold can be buried deep inside the protein’s structure and essentially invisible to the cell’s quality control system. With the small proteins there were fewer steps and less to hide behind so the mistakes could be quickly fixed. So, we simulated a normal size protein at the atomic scale and saw misfolding that persisted.”

The team also tracked folding of the proteins used in their simulations experimentally. While they couldn’t directly observe the misfolds in the experiments, structural changes inferred using mass spectrometry occurred in the locations that misfolded in their simulations.

“Most misfolded proteins are quickly fixed or degraded in cells,” O’Brien said. “But this type of entanglement presents two major problems. They are difficult to fix as they can be very stable, and they can fly under the radar of the cell’s quality control systems. Coarse-grain simulations suggest that this type of misfolding is common. Learning more about the mechanism can help us understand its role in aging and disease and hopefully point to new therapeutic targets for drug development.”

In addition to Vu and O’Brien, the research team includes Ian Sitarik, graduate student in chemistry; Yang Jiang, assistant research professor in chemistry; and Hyebin Song, assistant professor of statistics, at Penn State; Yingzi Xia, Piyoosh Sharma, Divya Yadav, and Stephen D. Fried at Johns Hopkins University; and Mai Suan Li at the Polish Academy of Sciences.

The U.S. National Science Foundation, the U.S. National Institutes of Health and the Polish National Science Centre funded the research. The research was supported in part by the TASK Supercomputer Center in Gdansk, Poland; the PLGrid Infrastructure in Poland; and the Roar supercomputer in the Institute for Computational and Data Sciences at Penn State.

Fighting off pathogens is a tour de force that must happen with speed and precision. A team of researchers at CeMM and MedUni Vienna led by Christoph Bock and Matthias Farlik has investigated how macrophages-immune cells that are the body’s first responders-master this challenge. Their study, published in Cell Systems (DOI: 10.1016/j.cels.2025.101346), offers a time-resolved analysis of the molecular processes that unfold when these cells encounter various pathogens. They developed a new method that combines gene editing and machine learning, which identified key regulators of macrophage immune responses.

Macrophages (Greek for “big eaters”) deserve their name: their job is to recognize invading pathogens such as bacteria or viruses, engulf them and break them down into their biochemical building blocks. Macrophages are also messengers: they release various signals to recruit other immune cells, trigger inflammation, and present digested fragments of pathogens on their surface, guiding the adaptive immune system to develop long-term immunity.

Macrophages encountering a pathogen are under immense pressure. If they react too late or not decisively enough, an infection may become fatal. But an overshooting immune response is equally damaging. Within a very short time, a tailored immune response must be initiated: cascades of biochemical reactions triggered, thousands of genes activated, and an arsenal of substances produced-each response tailored to the specific pathogen encountered.

Network of regulators uncovered

To understand how macrophages coordinate this multitude of tasks, the team led by Christoph Bock (CeMM Principal Investigator and Professor at MedUni Vienna) and Matthias Farlik (Principal Investigator at the MedUni Vienna) exposed macrophages from mice to various immune stimuli that mimic bacterial or viral infections. They tracked the changes inside the cells by measuring gene activity and DNA accessibility every few hours, establishing a molecular timeline of how the regulatory programs unfold step by step.

Next, the team identified regulatory proteins that orchestrate these programs, using CRISPR genome editing to produce hundreds of gene knockouts and single-cell RNA sequencing to characterize the genetically perturbed cells. This innovative method uncovered a network of several dozen regulators that share the responsibility of triggering the most appropriate immune response. The identified regulators include many “usual suspects” such as the JAK-STAT signaling pathway, but also splicing factors and chromatin regulators whose role in immune regulation is not well understood.

It is impressive how much complexity there is in this ancient part of our immune system, which we share with sponges, jellyfish and corals. Thanks to the advances in CRISPR screening technology, we can systematically study the underlying regulatory programs.”

Christoph Bock, senior author

In this review, the authors present recent findings that uncover a previously unappreciated nuclear signaling hub: the PIPn-p53 signalosome. This complex not only modulates AKT activation within the nucleus but also integrates two major oncogenic pathways-p53 dysregulation and PI3K-AKT amplification-into a unified mechanism driving cancer cell migration and invasion.

Key points of the review include:

1. Nuclear PIPn signaling expands beyond classical models: Phosphoinositides, long thought to be confined to plasma and endomembranes for cytoplasmic signaling, are now shown to form active signaling complexes in the nucleus, reshaping our understanding of lipid-mediated regulation.
2. Wild-type and mutant p53 serve as nuclear scaffolds: Both forms of p53 anchor nuclear PIPns and facilitate the assembly of lipid-protein complexes (signalosomes), directly influencing gene expression, chromatin remodeling, and cytoskeletal dynamics.
3. De novo AKT activation in the nucleus: Unlike canonical membrane-bound activation, nuclear AKT is activated by PtdIns(3,4,5)P₃ generated by the PIPn-p53 complex. This activation promotes cancer cell survival and migration-particularly under stress.
4. Therapeutic implications: Disruption of the nuclear PIPn-p53 signalosome, especially in mutant p53-driven cancers, could impair metastasis. Targeting nuclear-specific PIPn enzymes or restoring p53 function may synergize with PI3K/AKT inhibitors to suppress cancer dissemination.

This review highlights the nuclear PIPn-p53 signalosome as a central regulator of cancer cell motility and a promising target for metastasis therapy. The work entitled “The Nuclear Phosphoinositide-p53 Signalosome in the Regulation of Cell Motility” was published in Protein & Cell (Advance access May 26, 2025).

An international research team involving the Leibniz Institute on Aging – Fritz Lipmann Institute (FLI) in Jena, the Scuola Normale Superiore Pisa, and Stanford University has discovered that in the aging brain, certain proteins are lost even though their mRNA blueprints remain intact. The reason for the loss is not increased degradation, but rather a manufacturing error: ribosomes get stuck on sections rich of basic amino acids, preventing the production of important proteins needed for DNA repair and ribosome assembly. This finding provides new insights into brain aging and neurodegenerative diseases.

Proteostasis describes the balance of proteins in cells, which includes the continuous production of new proteins, their correct folding, and the degradation of damaged or redundant proteins. This balance is essential for cell health; if it is out of balance, misfolded or redundant proteins can accumulate—with potentially harmful consequences. Such dysfunctions are a typical feature of aging and are closely linked to diseases such as Alzheimer’s and Parkinson’s.

An international research team from the Leibniz Institute on Aging – Fritz Lipmann Institute (FLI) in Jena, the Scuola Normale Superiore in Pisa, and Stanford University has now investigated how the aging process influences proteostasis in the brain. In the process, they identified a central mechanism that disrupts proteostasis in the aging brain—with far-reaching consequences. The results have now been published in the journal “Science”.

Model organism killifish provides precise insights

The brain of the short-lived killifish (Nothobranchius furzeri), an established model organism in aging research that shows typical age-related changes in the brain, such as neurodegenerative processes, was investigated.

The team comprehensively analyzed how gene expression is regulated during aging—from the transcription of genetic information (transcriptome) to protein production by ribosomes (translatome) to the actual composition of the proteins formed (proteome). “This multi-step approach allowed us to determine very precisely at which level age-related changes occur and which mechanisms are disrupted,” explains Domenico Di Fraia, former graduate student of the FLI and co-first author of the study.

Protein loss despite intact blueprint

The study focused on a remarkable observation: many proteins, especially those with numerous basic amino acids (e.g., arginine, lysine), decreased significantly in the aging brain. These proteins play a central role in DNA and RNA processing and in the formation of ribosomes. Their absence can have far-reaching cellular consequences.

Surprisingly, the mRNA, i.e., the corresponding blueprint for these proteins, was present in normal amounts. “This was a clear sign to us that the problem lay not in the degradation but in the production of the proteins,” explains Alessandro Ori, associated research group leader at the FLI and senior author of the study.

Further analyses showed that the ribosomes—the cell’s “protein factories” that produce proteins from mRNA blueprints—became stuck on sequences containing basic amino acids. The ribosomes “paused” or even collided, preventing the corresponding protein from being completed correctly or even formed initially. This is an indication of a specific disorder of translation in the aging brain.

These disorders mainly affected proteins responsible for important central tasks such as DNA repair, RNA processing, cell division, and energy production in the mitochondria. They are therefore closely linked to many already known “hallmarks of aging”—typical biological characteristics of aging.

Translation disrupted – not protein degradation

To rule out the possibility that the protein loss was not based on increased degradation, the team specifically blocked the proteasome—the cellular “waste disposal system.” This ensures the quality of proteins by breaking down damaged, misfolded, or no longer needed proteins, thereby helping to maintain the function and stability of cellular processes.

“Although this changed the proteome, the loss of basic proteins remained. So, they were not degraded, but apparently not produced correctly in the first place. This confirmed our assumption that the cause lies at the level of translation— i.e., protein biosynthesis,” continued Antonio Marino, former graduate student of the FLI and co-first author of the study.

Chain reaction in the aging brain

Using an integrative model, it was also shown that reduced ribosome function during aging affects the production of certain proteins more than others. Some mRNAs are even read more efficiently because there are fewer “traffic jams,” while others are hardly read at all. This results in a kind of chain reaction: missing ribosomes promote further changes in translation and further contribute to modify the protein composition of old brains.

“Proteins in the mitochondria and nervous system are particularly affected,” adds Alessandro Ori. “This imbalance disrupts the balance of proteins in the brain and could be a possible trigger for age-related diseases such as Alzheimer’s or Parkinson’s.”

Groundbreaking findings for aging and dementia research

The study provides the first conclusive explanation for the phenomenon of mRNA and protein levels often no longer matching in the aging brain, which is also known to occur in humans. The reason is a malfunction in protein synthesis, in which ribosomes become stuck. “We have identified a weak point in the cellular machinery that increasingly fails with aging, “This malfunction could play a central role in the development of neurodegenerative diseases.”

These findings extend previous observations from studies in nematodes and show that translation disorders are a major factor in the decline of proteostasis in aging vertebrate brains.

In the long term, the findings could open up new possibilities for therapies that specifically prevent the loss of important proteins—and thus counteract neurodegenerative diseases.

 

Tom Hanks is remembering the late Jim Lovell.

Following the news that commander of Apollo 13 mission, Lovell died on Thursday at 97, Hanks, took to Instagram on Friday evening to share a tribute. Hanks famously played the astronaut in the 1995 film of the same name.

“There are people who dare, who dream and who lead others to the places we would not go on our own. Jim Lovell, who for a long while had gone farther into space and for longer than any other person of our planet, was that kind of guy,” Hanks wrote on his post. “His many voyages around Earth and on to so-very-close to the moon were not made for riches or celebrity, but because such challenges as those are what fuels the course of being alive — and who better than Jim Lovell to make those voyages.”

He continued, “On this night of a full moon, he passes on — to the heavens, to the cosmos, to the stars. Godspeed you, on this next voyage, Jim Lovell.”

The ’95 film follows the real-life story of astronauts Lovell (Hanks), Fred Haise (Bill Paxton) and Jack Swigert (Kevin Bacon) and their mission to the moon in 1970 that was called off after an oxygen tank exploded, which threatened their return to Earth. The movie won two Oscars, including best sound and best editing; it also received a nomination for best picture. The film is recognized as one of Hanks’ most memorable performances, and especially, his famous line is: “Houston, we have a problem.”

To also honor Lovell’s career, the film’s director, Ron Howard, paid tribute: “Rest in peace, Commander Lovell. Navy test pilot, Gemini 7, Gemini 12, Apollo 8 and, of course, Apollo 13. Simply knowing Jim has been a tremendous honor. His combination of intellect, courage and commitment to duty made him one of the most remarkable individuals I’ve ever met. His support of our movie-making efforts inspired authenticity and elevated our process in so many ways. Thank you, sir, for your service to our country and to humankind.”

Brian Grazer, a producer on the movie, called Lovell “a true American hero whose courage, intellect and grace under pressure inspired a nation.” He added, “He was not only a legend in space exploration, but also an incredibly generous, kind and inspiring man. Thank you, Commander Lovell, for showing us the best of what we can be.”

Additionally, NASA shared a statement, which reads: “Jim’s character and steadfast courage helped our nation reach the Moon and turned a potential tragedy into a success from which we learned an enormous amount. We mourn his passing even as we celebrate his achievements.”

Apollo 13 director Ron Howard and producer Brian Grazer paid tribute today to Jim Lovell, commander of the ill-fated moon mission on which they based their hit 1995 movie. The astronaut died Thursday at 97.

“Jim Lovell was a true American hero whose courage, intellect and grace under pressure inspired a nation,” Grazer said in a statement. “He was not only a legend in space exploration, but also an incredibly generous, kind and inspiring man. Thank you, Commander Lovell, for showing us the best of what we can be.”

Howard said: “Rest in peace, Commander Lovell. Navy test pilot, Gemini 7, Gemini 12, Apollo 8 and, of course, Apollo 13. Simply knowing Jim has been a tremendous honor. His combination of intellect, courage and commitment to duty made him one of the most remarkable individuals I’ve ever met. His support of our movie-making efforts inspired authenticity and elevated our process in so many ways. Thank you, sir, for your service to our country and to humankind.”

Lovell was 42 when led the moon shot that launched April 11, 1970, but never made its scheduled landing. An oxygen tank explosion two days into the flight took out crucial systems and turned the mission into a rescue operation. NASA scientists made a plan to use the moon’s gravity as a slingshot to send the spacecraft back to Earth, where it splashed down four days later.

Apollo 13 is a gripping tale of what happened up there 45 years ago and how a calm but stressed NASA team brought them home, against the odds. The film was an international smash, making $355.2 million worldwide, split almost evenly between domestic and international. It starred Tom Hanks as Lovell, alongside Kevin Bacon and Bill Paxton as fellow astronauts Jack Swigert and Fred Haise, respectively. Ed Harris and Gary Sinise also starred, along with Kathleen Quinlan as Lovell’s wife Marilyn.

Hanks was hot off back-to-back Best Actor Oscars for Philadelphia and Forrest Gump when he portrayed Lovell. The actor posted a tribute of his own on Instagram today that reads: “There are people who dare, who dream and who lead others to the places we would not go on our own. Jim Lovell, who for a long while had gone farther into space and for longer than any other person of our planet, was that kind of guy. His many voyages around the Earth and on to so-very-close to the moon were not made for riches or celebrity, but because such challenges as those are what fuels the course of being alive — and who better than Jim Lovell to make those voyages. On this night of a full moon, he passes on — to the heavens, to the cosmos, to the stars. God speed you, on this next voyage, Jim Lovell.”

In this week of R&D updates, we witness the cosmos revealing life’s building blocks in unexpected places, while down on Earth, GPT-5 launched, the model that has been in development since March 2023. Also, potentially breakthrough treatments offer hope for devastating diseases and quantum discoveries challenge our understanding of reality. This week’s developments range from practical (new medical treatments) to fundamental (quantum states of matter).

Quantum computing and physics

Columbia engineers enable quantum computer sharing with HyperQ

The story: Scientists at Columbia Engineering have developed a new system that enables multiple users to share a single quantum computer simultaneously using isolated quantum virtual machines (qVMs). They call the system HyperQ.

The numbers:

• HyperQ reduced user wait time by 40-fold
• Project timelines shorten from days to hours

Why it matters: Most quantum computers can only support single-user applications due to the interconnection between qubits. The researchers solved this problem by isolating each qVM with a buffer of inactive qubits, preventing them from interfering with one another.

Watch for: The team intends to expand HyperQ to function across quantum computing architectures.

Scientists discover quantum liquid crystal state of matter

The story: Rutgers University scientists discovered a new quantum state called “quantum liquid crystal” by combining Weyl semimetal with spin ice materials under extreme magnetic fields. Published in Science Advances, this marks the first observation of electronic anisotropy at a heterostructure interface.

The numbers:

• Electronic anisotropy in exactly 6 specific directions
• Electrons flow in precisely 2 opposite directions under increased magnetic fields
• Zero energy loss electrical conduction due to Weyl fermions
• 4+ years spent developing the custom Q-DiP platform

Why it matters: This breakthrough enables design of ultra-sensitive quantum sensors for extreme environments like space and powerful machines. The zero-loss conduction could have implications for electronics for quantum computing.

Watch for: Expansion to other quantum material combinations and development of practical applications in quantum sensors and advanced electronics.

Materials science and physics

Scientists superheat gold past melting point without liquefying

The story: Scientists used an ultrafast high-intensity laser to superheat gold past its melting point without turning it into a liquid. Their findings were published in Nature.

The numbers:

• The gold was heated to 14 times its melting point (19,000 kelvin / 33,700°F)
• Gold’s melting point is 1,337 kelvin (1,947°F)
• They used 45 femtosecond (45 quadrillionths of a second) X-ray laser pulses

Why it matters: It has been challenging for scientists to measure the temperature of unusual states of matter like plasma, called “warm dense matter”. These findings could help scientists find a new way to accomplish this.

Watch for: Bob Nagler, the lead author of the study, plans to apply the new measurement technique to inertial fusion energy research at the Department of Energy’s SLAC National Accelerator Laboratory.

AI and computing

OpenAI and Anthropic drop new AI models

The story: While AI bubble talk remains a theme, frontier AI labs continue to launch new models at a rapid clip. OpenAI launched gpt‑oss‑120b (117B parameters) and gpt‑oss‑20b (21B parameters), the first open-weight release since GPT‑2. The open-weight models activate a fraction of their parameters in use. Gpt-oss-120b activates 5.1B parameters per token, while gpt-oss-20b activates 3.6B, according to OpenAI. Meanwhile, Anthropic launched Claude Opus 4.1, an incrementally improved version of its largest model, and OpenAI announced the much-delayed GPT-5, which has received mixed reviews immediately after launch.

The numbers:

• 117B and 21B: Parameter counts for OpenAI’s new open-weight models
• 74.5%: Claude Opus 4.1’s score on the SWE-Bench Verified coding benchmark
• 45–80%: Reported reduction in hallucinations in GPT-5 compared with GPT-4o and o3 models, respectively.
• 5.1B parameters per token activated in gpt-oss-120b (3.6B in gpt-oss-20b)

Why it matters: GPT‑5’s launch signals a jump in AI reasoning and usability with reportedly fewer hallucinations. Anthropic’s Claude Opus 4.1 reinforces its dominance in AI-powered coding tools, while OpenAI’s open-weight models democratize access to powerful AI capabilities.

Watch for: Whether GPT‑5 can retain leadership in coding and reasoning as enterprises test it against Claude and other agents. Opus 4.1 may force OpenAI to respond with targeted improvements or pricing strategy.

Space and cosmology

Complex organic molecules detected in planet-forming disk

The story: Astronomers using the ALMA telescope have detected 17 complex organic molecules in the protoplanetary disk around V883 Orionis, marking the first time such complex chemistry has been found in a planet-forming environment. The molecules include ethylene glycol, glycolonitrile, and precursors to amino acids glycine and alanine, plus adenine—a fundamental building block of DNA.

The numbers:

• 17 complex organic molecules detected, including life’s building blocks
• Star is located 1,305 light-years away
• V883 Orionis is only 500,000 years old (compared to our Sun at 4.6 billion years)
• Detection enabled by stellar outbursts heating the disk from -263°C to -173°C

Why it matters: This discovery challenges the “chemical reset” theory that complex molecules are destroyed during star formation. Instead, it suggests life’s building blocks are inherited from interstellar space and may be widespread throughout the cosmos.

Watch for: The research team plans higher resolution observations to confirm tentative detections. Future James Webb Space Telescope observations could reveal whether similar chemistry exists in other star-forming regions.

NASA’s acting administrator calls for nuclear reactor on the Moon

The story: NASA’s Acting Administrator Calls for a Nuclear Reactor on the Moon,  NASA is pushing forward with plans to establish nuclear power infrastructure on the lunar surface as part of its Artemis program and long-term lunar habitation goals.

Why it matters: Nuclear power could provide the consistent energy needed for lunar bases, life support systems, and in-situ resource utilization, enabling sustained human presence on the Moon.

Watch for: Development of compact, transportable nuclear reactor designs suitable for the harsh lunar environment.

Medicine and biotechnology

FDA approves first treatment for rare aggressive brain cancer

The story: The FDA granted accelerated approval on August 6, 2025, to Jazz Pharmaceuticals’ Modeyso (dordaviprone), the first and only systemic therapy for H3 K27M-mutant diffuse midline glioma. This devastating brain cancer primarily affects children and young adults who typically survive only one year after diagnosis.

The numbers:

• 22% overall response rate in clinical trials
• 10.3 months median duration of response
• 73% of responders maintained response for at least 6 months
• 27% maintained response for at least 12 months
• Affects approximately 2,000 people annually in the US

Why it matters: This addresses an urgent unmet medical need for a uniformly fatal pediatric brain cancer with no previous approved treatments. The drug works through a novel mechanism as a protease activator targeting mitochondrial caseinolytic protease P.

Watch for: The Phase 3 ACTION confirmatory trial measuring overall survival in 450 patients will determine continued approval. Commercial availability is immediate, offering hope to families facing this devastating diagnosis.

RFK Jr. cancels mRNA vaccine grants amid declining vaccination rates

The story: RFK Jr. canceled grants and contracts to develop mRNA vaccines on Tuesday. Simultaneously, children’s vaccine rates are dipping. The CDC reported that kindergarteners’ vaccine coverage decreased in 2024-25 compared to the year before.

The numbers:

• The total number of canceled grants and contracts is nearly $500 million
• 286,000 children attended kindergarten without receiving the MMR vaccine
• Vaccine exemptions increased from 3.3% to 3.6%, with some states exceeding 5%
• A study from UCLA Health found that almost 9 in 10 ER patients have not received one or more recommended vaccinations

Why it matters: Canceled grants could decrease vaccine availability. The HHS said it will favor other vaccines over those using mRNA, an outdated approach. Some scientists have said this could threaten public safety.

Watch for: Further restrictions on vaccines by RFK, continuing decrease of vaccination rates, decrease of vaccine availability and slow vaccine releases.

New implant offers hope for easing rheumatoid arthritis

The story: New Implant Offers Hope for Easing Rheumatoid Arthritis – Researchers have developed a novel implant that stimulates the vagus nerve to reduce inflammation in rheumatoid arthritis patients, offering a drug-free treatment alternative.

Why it matters: This bioelectronic medicine approach could provide relief for patients who don’t respond well to conventional treatments or want to avoid long-term medication side effects.

Watch for: Clinical trial results and potential expansion to other inflammatory conditions.

Desalination system could produce freshwater cheaper than tap water

The story: Desalination system could produce freshwater that is cheaper than tap water – MIT researchers have developed a new desalination system that could produce freshwater at costs lower than municipal tap water, potentially solving water scarcity challenges.

Why it matters: With growing global water stress, affordable desalination could provide reliable freshwater access to billions while being economically viable for widespread deployment.

Watch for: Pilot projects and scaling efforts to bring this technology to water-stressed regions worldwide.

Synthetic biology

E. coli engineered with 57-codon genetic code

The story: Escherichia coli with a 57-codon genetic code. Scientists have successfully created E. coli bacteria with a compressed genetic code using only 57 codons instead of the standard 64, demonstrating unprecedented control over biological systems.

Why it matters: This achievement opens new possibilities for creating organisms resistant to viral infection and capable of producing novel proteins with non-natural amino acids, with potential applications in biotechnology and pharmaceutical production.

Watch for: Applications in industrial biotechnology and development of virus-resistant organisms for pharmaceutical manufacturing.