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Compact CRISPR system unlocks targeted in-body gene editing, with up to 90% efficiency

A research team has discovered an enhanced CRISPR gene-editing system that could enable targeted delivery inside the human body—a key step toward broader clinical use. Researchers identified a naturally occurring enzyme, Al3Cas12f, that is small enough to fit into adeno-associated virus vectors, a leading targeted delivery method for gene therapies. They then engineered an enhanced version that dramatically improved gene-editing performance in human cells.

The advance addresses a major limitation in CRISPR technology. Commonly used gene-editing proteins are too large for targeted delivery systems, restricting clinical applications to cells modified outside the body, such as blood and bone marrow.

“Smart delivery of gene editing systems is a powerful notion with broad clinical implications, and this basic science finding takes us a significant step toward that future,” said Erica Brown, Ph.D., acting director of NIH’s National Institute of General Medical Sciences (NIGMS).

Protein clusters reshape cell movement and may help cells build amino acids faster

Cells can be thought of as cities, with factories, a transport system, and lots of building activity. An international team led by scientists at the University of Groningen studied cells growing under different conditions and measured the speed of molecule transport. They found that some conditions led to changes in the mobility inside the cells, caused by the clustering of proteins that produce the building materials for growth. It could be that clustering enables the proteins to produce those building blocks more efficiently. The research is published in the journal Molecular Cell.

The research started with a seemingly simple question. How much movement is there within a cell? “We provided bacteria with different nutrients and this resulted in different growth rates,” explains Matthias Heinemann, Professor of Molecular Systems Biology. Movement was measured by inserting tiny (40 nanometers) fluorescent particles in the cells that could be tracked under the microscope. “To our surprise, we found that particle movement under different conditions could vary by a factor of three.”

The scientific literature could not explain this observation. By analyzing the cell content, the scientists found a correlation between movement of the fluorescent particles and the number of proteins that are involved in the production of amino acids. “More of these proteins meant less movement inside the cell,” says Heinemann. “This led us to the question of why this happens. Our hypothesis was that these proteins form clusters that act as obstacles to movement inside the cells.”

A tabletop ring of atoms brings the universe’s doomsday vacuum collapse into the lab

Physicists in China have simulated the effect of “false vacuum decay”: a phenomenon believed to play out constantly in the seemingly empty expanses of space, and which one theory even suggests could bring an abrupt end to the entire universe. In a paper published in Physical Review Letters, Yu-Xin Chao and colleagues at Tsinghua University, Beijing, mimicked the effect using a simple tabletop experiment.

For now, quantum field theory is our most accurate framework for fundamental physics below the scale at which gravity becomes important. It predicts that there is no such thing as a perfect vacuum: while a given space may appear entirely empty, the theory suggests that it is actually just the lowest-energy state of a continuous quantum field.

Since a quantum field can possess multiple local minima energy, this means that a seemingly stable local ground state may not be the most stable state possible for the field as a whole—it is simply separated from a lower-energy, more stable state by an energy barrier, much as a valley may be separated from a deeper valley by a high mountain ridge.

Phase-changing VO₂ turns methane into propane and hydrogen more efficiently

Converting methane, the primary component of natural gas, into higher alkanes and hydrogen, could be highly advantageous. Alkanes, such as propane and butane, are easier to transport than methane and are used in a wider range of industries. Hydrogen, on the other hand, is a promising clean fuel used to power electrochemical devices that can generate continuous power, known as fuel cells.

Over the past decades, some energy engineers have been exploring the possibility of converting methane into hydrogen or complex hydrocarbons using photocatalysts. These are materials activated by sunlight or other types of light and that can drive chemical reactions.

Researchers at Université de Lille—CNRS, Sorbonne Université and other institutes in France recently introduced a new strategy for the photocatalytic conversion of methane into propane, which is widely used for heating, cooking, and transportation.

Low-frequency wireless sensor tracks artery stiffening in real time with less interference

Wireless sensors used in wearable smart devices and medical equipment must be capable of detecting minute changes while maintaining high operational stability. However, existing technologies often utilize excessively high frequencies, leading to electromagnetic interference (EMI) or potential health risks to the human body. To address these fundamental issues, a Korean research team has developed a low-frequency-based wireless sensor technology.

A joint research team, led by Professor Seungyoung Ahn from the KAIST Cho Chun Shik Graduate School of Mobility and Professor Do Hwan Kim from the Department of Chemical Engineering at Hanyang University, has developed the “WiLECS” (Wireless Ionic-Electronic Coupling System), a low-frequency wireless electrochemical sensing platform that combines ion-based materials with wireless power transfer technology. The research is published in the journal Nature Communications.

Conventional wireless sensors suffer from low capacitance (the ability to store electrical charge), requiring high frequencies in the megahertz (MHz) range to compensate. However, these high-frequency methods can cause tissue heating or signal instability, limiting their practical application in clinical medical settings.

Pain-sensing neurons mapped in unprecedented detail, pointing to new chronic pain drug targets

One in five people worldwide suffers from chronic inflammatory pain. Meanwhile, about two thirds of those affected find little relief from existing pain medications; new therapeutic approaches are urgently needed. “We first must understand precisely how sensory nerve cells trigger pain at the molecular level—in other words, which proteins are involved,” says Professor Gary Lewin, Group Leader of the Molecular Physiology of Somatosensory Perception lab at the Max Delbrück Center in Berlin.

To unravel these molecular processes, Lewin—who has been studying pain for four decades and recently discovered a previously unknown ion channel involved in pain perception—is working closely with systems biologist Dr. Fabian Coscia, Group Leader of the Spatial Proteomics lab at the same center. Coscia co-developed a method called Deep Visual Proteomics that makes it possible to determine the proteome —the complete set of proteins—of specific cells and to create maps detailing the spatial locations of individual proteins.

The researchers combined this technology with electrophysiological methods from Lewin’s group. This enabled them to first identify specific subtypes of pain neurons based on their function and then analyze their protein profiles. The result is a high-resolution molecular map of these nerve cells, which has been published in Nature Communications. The team also demonstrated how the technology can identify potential new drug targets to treat chronic pain.

Math model reveals how life may have switched on from Earth’s primordial soup

Isolating the first spark of life on Earth is a matter of biology, geology, and chemistry—but it’s also an amazing math problem. At least, that’s how Varun Varanasi viewed it when he was a Yale undergraduate. The question, in a nutshell, is this: How did the primordial soup of interacting molecules on the Earth’s surface billions of years ago transform itself from complete chaos to an organized system of self-sustaining, reproducing chemicals? Did this occur gradually over millions of years, or was it abrupt?

Self-interacting dark matter may solve three cosmic puzzles

A study led by UC Riverside physicist Hai-Bo Yu suggests that a new type of dark matter could explain three astrophysical puzzles across vastly different environments. Published in Physical Review Letters, the study proposes that dense clumps of self-interacting dark matter (SIDM)—each about a million times the mass of the sun—can account for unusual gravitational effects observed in gravitational lenses, stellar streams, and satellite galaxies.

Dark matter, which makes up about 85% of the universe’s matter, cannot be seen directly. The standard model assumes it is “cold” and collisionless, meaning that particles pass through one another without interacting. This model struggles, however, to explain certain high-density structures observed in the universe.

Yu’s work instead focuses on SIDM, in which dark matter particles collide and exchange energy. These interactions can trigger “gravothermal collapse,” forming extremely dense, compact cores.

Designing better membrane proteins by embracing imperfection

Scientists at the VIB–VUB Center for Structural Biology have uncovered a counterintuitive principle that could reshape how membrane proteins are designed from scratch: Sometimes, making a protein less stable helps it fold correctly. In their study published in the Proceedings of the National Academy of Sciences, the researchers demonstrate that introducing carefully placed “imperfections,” a strategy known as negative design, enables synthetic membrane proteins to fold and assemble efficiently in artificial membranes.

Membrane proteins are essential for life and biotechnology, acting as gateways, sensors, and drug targets. Yet designing them from scratch remains notoriously difficult. Unlike soluble proteins, they must navigate a complex folding process while inserting into lipid membranes and during this step, many designs fail.

Traditional protein design focuses on maximizing the stability of the final folded structure. But the new study shows that, for transmembrane β-barrel proteins, this approach can backfire.

‘Ghost tunnels’ guide sound waves in one direction while staying invisible to others

Acoustic metamaterials are a fast-evolving family of materials which manipulate sound waves in ever more advanced ways. Now, a team led by Changqing Xu at Nanjing Normal University in China has engineered an acoustic metamaterial, a “ghost tunnel”: a structure which acts as a near-perfect waveguide for sound entering through its ends, while being essentially invisible to waves incident on its sides. The results, published in Physical Review Letters, could open new avenues for manipulating sound waves in complex signal environments.

Acoustic waveguides work by confining sound within a channel, using boundaries that reflect waves back inward to keep them on track. While this can be achieved with a structure as simple as a hollow pipe, the problem is that those same reflective boundaries inevitably interact with any sound waves approaching from outside the channel.

Rather than passing through undisturbed, external waves scatter off the rigid walls: a significant drawback in technologies where multiple signal channels must coexist in close proximity without interfering with one another.

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