Scientists finally see DNA “zip” itself together for the first time

 

DNA strands zipping together. Credit: Professor Agnes Noy, University of York

DNA carries a negative electrical charge. Because objects with the same charge normally push away from each other, DNA molecules might be expected to repel one another. Yet inside living cells, DNA must sometimes come into close contact and recognize matching sequences. These interactions are essential for processes including genetic recombination and gene silencing, and they can also play a role in cancer.

Scientists have now captured a remarkably detailed view of how this happens. Using powerful atomic force microscopy, researchers watched short pieces of DNA align with extraordinary precision, matching one another groove for groove. Computer simulations then revealed what appears to make this close contact possible: positively charged metal ions can settle into the grooves of DNA and serve as tiny molecular bridges between the two molecules.

Tiny Ions Help DNA Overcome Repulsion

Professor Agnes Noy, from the School of Physics, Engineering and Technology at the University of York, co-led the research. She said: "This discovery could help researchers identify regions of the genome specially involved in DNA pairing. These regions may become particularly important when mutations disrupt normal cellular processes and contribute to cancer."

The results provide experimental support for an idea proposed about twenty years ago called the "DNA zipper" model. Professor Alexey Kornyshev from Imperial College London and his collaborators originally suggested that salt ions surrounding DNA could produce alternating patterns of electrical charge. Those patterns, according to the model, would help neighboring DNA molecules align with one another much like two interlocking spiral staircases.

Until now, directly observing this proposed mechanism had proved difficult.

Scientists Put the "DNA Zipper" to the Test

To investigate the process, the researchers scanned DNA samples with atomic force microscopy, a technique capable of mapping surfaces at extremely small scales. These scans allowed the team to construct detailed topographical maps showing how the DNA molecules were positioned.

At the same time, sophisticated computer simulations followed individual atoms and ions as they moved around the DNA. Combining the two approaches gave researchers both a direct view of DNA pairing and a way to understand the molecular forces responsible for it.

The simulations showed that double-charged metal ions can effectively behave like two charged arms. Each ion can interact with both DNA molecules at once, forming a bridge across the space separating them and helping hold the two strands in alignment.

Dr. Thomas Catley, co-lead author from the School of Chemical Materials and Biological Engineering at the University of Sheffield, said: "It was incredible to be able to directly visualize the long-hypothesized mechanism for the first time. The advanced imaging techniques at our disposal are allowing us to uncover these key DNA interactions which have implications in many key cellular processes."

Dr. Victor Velasco-Berrelleza from the University of Sheffield, who performed the simulations, added: "Microscopy shows us what happens, but the simulations allow us to uncover the molecular mechanism behind it."

Some DNA Sequences Pair More Strongly

The researchers also found that DNA does not pair equally well along every sequence. Some stretches of DNA created much stronger contacts than others, producing distinct hotspots where two helices were especially likely to line up.

That finding could help researchers pinpoint parts of the genome that are particularly involved in DNA recognition and pairing. Such regions may become especially significant when mutations interfere with normal cellular activity and contribute to cancer.

The discovery could also have uses beyond medicine. Because some DNA sequences can be programmed to interact more strongly than others, scientists may eventually be able to take advantage of these properties to build customized DNA structures for biotechnology.

The study, "Imaging and mechanism of DNA-DNA recognition mediated by divalent ions," was published in the journal Nucleic Acids Research.

 

Journal Reference:

1. Thomas E Catley, Victor Velasco-Berrelleza, Daniel E Rollins, Alice L B Pyne, Agnes Noy. Imaging and mechanism of DNA–DNA recognition mediated by divalent ions. Nucleic Acids Research, 2026; 54 (16) DOI: 10.1093/nar/gkag817

Courtesy:

University of York. "Scientists finally see DNA “zip” itself together for the first time." ScienceDaily. ScienceDaily, 14 September 2026. <www.sciencedaily.com / releases / 2026 / 09 / 260909231717.htm>. 

 

Your sleep may be hiding an early clue to Alzheimer’s

 Could subtle changes during sleep reveal vulnerability to Alzheimer's disease years before memory problems become noticeable? Researchers at ULiège, supported by the Stop Alzheimer's Foundation, are investigating whether the sleeping brain may contain early clues.

Scientists from the University of Liège (GIGA Neurosciences) examined sleep patterns in more than 500 healthy people. Among participants in middle age, more frequent nighttime micro awakenings were associated with a higher genetic risk of developing Alzheimer's disease. That relationship was not detected among younger adults.

The findings, published in the journal Sleep, raise the possibility that sleep measurements could eventually help researchers identify people who may be more vulnerable to Alzheimer's before symptoms develop.

Looking for Alzheimer's Clues Before Symptoms

Researchers have spent years investigating connections between disturbed sleep and neurodegenerative diseases. The University of Liège study adds another piece to that research by suggesting that the relationship between sleep and Alzheimer's risk may begin well before recognizable symptoms emerge.

Because genetics play a partial role in Alzheimer's disease (Alzheimer's disease is neither purely hereditary nor entirely independent of genes), the researchers calculated a polygenic risk (i.e., summarizing the combined influence of your genes on your probability of developing a given disease in a single figure) for more than 500 healthy participants.

Most were young adults (aged 18 to 31), while the study also included an older group (aged 50 to 69). Importantly, the polygenic risk measured in the study remained low and cannot determine whether any particular person will eventually develop Alzheimer's disease.

The researchers then compared these genetic risk estimates with different characteristics of each participant's sleep.

Tiny Awakenings During the Night

The analysis revealed an association between genetic risk for Alzheimer's disease and the frequency of nighttime micro awakenings. These are very brief bursts of brain activity that can interrupt the normal sleep cycle without causing someone to become fully awake.

Among the younger participants, researchers found no connection between these micro awakenings and Alzheimer's genetic risk. A different pattern appeared in the older group. Participants who experienced more frequent micro awakenings also tended to have higher genetic risk, despite being healthy, relatively young and free of Alzheimer's symptoms.

"These micro-awakenings are therefore not insignificant," emphasizes Puneet Talwar, a researcher at the GIGA ULiège laboratory, "certain profiles could promote the accumulation of proteins involved in Alzheimer's disease and be associated with increased vulnerability."

A Tiny Brain Region Draws Attention

The researchers also examined the locus coeruleus, a tiny area deep within the brainstem that is roughly the size of a grain of rice. It plays an important role in regulating wakefulness, attention, and sleep.

"This region is difficult to observe, but it appears to play a role in the early mechanisms linked to the disease," explains Gilles Vandewalle, co-director of the GIGA CRC In Vivo Imaging technology platform and Fund for Scientific Research - FNRS Research Director at ULiège.

In 2025, a preliminary study carried out with the 7-Tesla MRI scanner at the ULiège platform allowed the team to examine the locus coeruleus in greater detail. The researchers found that characteristics of sleep quality (speed of falling asleep, depth) were associated with the condition of the brainstem beginning at a young age.

They also found that healthy functioning of the locus coeruleus was related to the quality of REM sleep, a stage of sleep that plays an important role in memory.

The locus coeruleus is especially interesting to Alzheimer's researchers because it is among the earliest brain regions where abnormal protein deposits can appear. Such deposits may begin accumulating as early as adolescence, although scientists still do not fully understand what these early changes mean.

Could Sleep Become an Early Alzheimer's Marker?

Taken together, the findings point toward possible new approaches for Alzheimer's screening and prevention. In the future, analyzing sleep could potentially complement other methods for identifying people who may be vulnerable to the disease before symptoms become apparent.

"Sleep could become an accessible marker for the early identification of vulnerable individuals," adds Gilles Vandewalle.

Researchers are also interested in whether improving sleep could eventually help prevent or slow disease progression among people with a genetic predisposition to Alzheimer's.

"This research shows that sleep is not only an indicator of health, but also a potential lever for intervention," adds Lucie Leroux, head of French-speaking activities at the Stop Alzheimer's Foundation.

More than 220,000 people in Belgium are affected by Alzheimer's disease. For now, however, the new findings show statistical associations rather than proof that particular sleep patterns cause or predict the disease. Additional research will be needed to confirm the results, and the findings cannot currently be used to determine whether an individual will develop Alzheimer's.

Even so, the research provides another glimpse into changes that may occur long before Alzheimer's becomes clinically visible and underscores the value of basic research aimed at understanding and, eventually, anticipating the disease.

Journal Reference:

1. Nasrin Mortazavi, Puneet Talwar, Ekaterina Koshmanova, Roya Sharifpour, Elise Beckers, Alexandre Berger, Islay Campbell, Ilenia Paparella, Fermin Balda, Ismael Dardour Hamzaoui, Christian Berthomier, Christine Bastin, Christophe Phillips, Pierre Maquet, Fabienne Collette, Mikhail Zubkov, Laurent Lamalle, Gilles Vandewalle. REM sleep quality is associated with balanced tonic activity of the locus coeruleus during wakefulness. Journal of Biomedical Science, 2025; 32 (1) DOI: 10.1186/s12929-025-01127-9

Courtesy:

University of Liège. "Your sleep may be hiding an early clue to Alzheimer’s." ScienceDaily. ScienceDaily, 28 August 2026. <www.sciencedaily.com/releases/2026/08/260828005218.htm>. 

 

 

 

 

 

 

A cancer therapy put severe rheumatoid arthritis into remission

 Immunotherapies such as CAR T-cell therapy were originally developed mainly to fight cancer. But scientists are now investigating whether these personalized treatments, made from a patient's own immune cells, could also help treat or even potentially cure autoimmune diseases.

Researchers at Charité - Universitätsmedizin Berlin have now tested CAR T-cell therapy in six people with particularly severe rheumatoid arthritis. The world's first clinical trial of its kind, reported in Nature Medicine, produced encouraging early results. Disease activity fell substantially in every participant, and by the end of the observation period, three patients no longer needed rheumatoid arthritis medication.

Why Rheumatoid Arthritis Can Be So Difficult To Treat

Rheumatoid arthritis is a chronic autoimmune disease in which the immune system mistakenly attacks the joints. Repeated inflammation causes swelling and can eventually damage the joints.

Existing medications are often effective at controlling inflammation, but they generally do not cure the disease. As a result, many patients need lifelong treatment with anti-inflammatory drugs and medications that suppress the immune system, which can also cause side effects.

For some people, even newer therapies do not work well enough. Doctors describe these cases as treatment-refractory rheumatoid arthritis. Patients can continue to experience pain, limited mobility, and major reductions in quality of life despite trying multiple treatments.

"One reason could be disease-driving B cells - memory cells of the adaptive immune system that may survive in the lymph nodes, bone marrow or joint tissue after an infection, where they produce harmful antibodies directed against the body's own tissues and repeatedly reignite the inflammation," explains Prof. David Simon, who designed the trial for this patient group together with Prof. Gerhard Krönke at Charité's Department of Rheumatology and Clinical Immunology.

The researchers are testing whether CAR T cells can seek out these disease-driving B cells even when they are buried deep within body tissues. Their goal is to eliminate as much of the abnormal B-cell memory as possible and effectively give the B-cell system a new start.

Using Cancer Immunotherapy To Reset the Immune System

CAR T cells were first developed as a cancer treatment, but their potential uses are expanding. In cancer therapy, a patient's immune cells are modified so they can recognize and destroy tumor cells. For autoimmune diseases, scientists instead want to direct those engineered cells toward immune cells that help sustain the disease.

"The identifying marker on many B cells, both abnormal B cells in cancers of the blood or lymphatic system and disease-driving B cells in rheumatoid arthritis, is the surface molecule CD19. You could think of it as a kind of 'name tag'," explains David Simon. "To enable CAR T cells to detect and eliminate the disease-causing cells, we equip patients' own immune cells with a receptor that acts like a search sensor for CD19."

To produce this form of CD19 CAR T-cell therapy, doctors first collect T cells from the patient's blood. T cells are immune cells that normally help recognize and destroy infected or abnormal cells.

Scientists then genetically modify those T cells in the laboratory. The cells receive a chimeric, or artificial, antigen receptor known as a CAR, which is designed to bind specifically to CD19.

Before receiving the modified cells, patients undergo a short course of preparatory chemotherapy. This temporarily lowers the number of certain immune cells, creating room for the CAR T cells to multiply and function effectively.

The engineered cells are then returned to the patient in a single infusion. Once inside the body, they search for cells carrying CD19 and attack them. This temporarily removes all CD19-positive B cells, including long-lived disease-driving cells in the joints that can otherwise be difficult to reach. By clearing out those cells, the treatment may allow the immune system to reset.

First Trial in Severe Rheumatoid Arthritis

For the first clinical trial evaluating both the safety and effectiveness of CD19 CAR T-cell therapy in rheumatoid arthritis, the Charité team initially enrolled six patients with especially severe disease.

The group included three women and three men between the ages of 31 and 69. During the previous decade, they had received as many as eight targeted or biologic therapies, but none had controlled their disease adequately.

Researchers wanted to learn whether CAR T cells could reach the disease-driving B cells inside the joints and whether the approach could do so safely.

The first phase of the COMPARE trial produced results the team considers highly encouraging.

"Disease activity decreased markedly in all six patients. During follow-up of up to one year, three patients were in sustained remission without any medication for rheumatoid arthritis," reports Gerhard Krönke, who leads the joint Clinical Rheumatology research group at Charité and the German Rheumatology Research Center (DRFZ), a Leibniz Institute. "This is particularly remarkable given that none of the established treatments had previously been able to relieve their symptoms adequately."

CAR T Cells Reached Hidden Disease Reservoirs

The treatment appeared to do more than temporarily reduce inflammation in the joints. Researchers found that the modified immune cells also reached and eliminated disease-promoting B cells in deeper locations, including the bone marrow, lymph nodes, and joint tissue.

During regular follow-up visits over the following 12 months, levels of the autoantibodies associated with rheumatoid arthritis dropped sharply.

David Simon adds: "When the B-cell system later recovered, predominantly naïve B cells that had not yet been shaped by the disease returned. In contrast, the B cells directed against the body's own tissues that had been present before treatment were no longer detectable in almost all patients, an indication that the treatment may indeed be able to reset the pathological immune memory."

Importantly, antibodies generated by earlier vaccinations, including those against chickenpox and tetanus, could still be detected. That suggests protective antibody memory was largely preserved even though the therapy caused a profound temporary depletion of B cells.

Researchers still need to determine whether the therapy has any longer-term effects on the immune system.

Promising Results, but the Therapy Remains Experimental

The trial suggests that a single CAR T-cell treatment can, in some patients, produce a sustained period without symptoms or rheumatoid arthritis medication. This state of disease inactivity is known as remission.

For carefully selected patients whose rheumatoid arthritis does not respond adequately to available treatments, researchers hope it may eventually be possible to directly reset pathological immune memory and stop the ongoing inflammation rather than continuously suppressing it with medication.

However, CAR T-cell therapy for autoimmune diseases, including rheumatoid arthritis, is still experimental. Researchers do not yet have long-term experience with the treatment.

Responses also differed among the six participants. Some did not achieve a complete response, and one patient's disease returned after an initial period of medication-free remission.

So far, however, the researchers consider the safety findings encouraging.

"After the participants received the CD19 CAR T cells, we observed only a temporary, mild-to-moderate cytokine release syndrome (CRS) in all participants, which was readily manageable. There were no severe neurological complications or other serious adverse events, and infections were rare," explains Dr. Marie Luise Hütter-Krönke, Medical Director of the Hematology Early Clinical Trial Unit at Charité's Department of Hematology, Oncology and Cancer Immunology.

A Larger Comparison Is Next

The second phase of the trial will include ten additional patients. Researchers plan to compare CAR T-cell therapy with an already approved rheumatoid arthritis drug that also targets B cells.

The comparison should help determine whether CAR T cells produce stronger or longer-lasting effects and whether they truly reset immune memory.

If these results are confirmed in this phase and in future larger studies, CAR T-cell therapy could eventually offer another option for people with severe rheumatoid arthritis whose lives are significantly affected by the disease and who currently have no adequate treatment.

About the Study

The first of the two phases of the COMPARE study was designed to assess the safety and effectiveness of CD19 CAR T-cell therapy in treatment-refractory rheumatoid arthritis.

Major contributors included researchers from Charité's Department of Rheumatology and Clinical Immunology and the Department of Hematology, Oncology and Cancer Immunology at Campus Benjamin Franklin, along with scientists from the Cluster of Excellence ImmunoPreCept, the German Rheumatology Research Center (DRFZ), a Leibniz Institute, and the Fraunhofer Institute for Translational Medicine and Pharmacology ITMP.

The study was initiated and designed at Charité and also received support from Kyverna Therapeutics. The immunotherapy company had no role in designing the study, collecting or analyzing the data, or presenting the results.

Journal Reference:

1. Fredrik N. Albach, Marie C. Rehm, Marie Luise Hütter-Krönke, Thanh Hang Le, Julia M. Giezen, Murat Torgutalp, Arne Sattler, Ioanna Minopoulou, Robert Biesen, Edgar Wiebe, Vincent Casteleyn, Thorben Witte, Christian Furth, Jan Zernicke, Melanie Nuesch Germano, Johan Verhagen, Artur Wilhelm, Maria Dzamukova, Klaus Engel, Simon Schallenberg, Aimo Kannt, Nicole Ziegler, Michaela Fehringer, Udo Schneider, Nadine Unterwalder, Mark Beling, Alexander Pfeil, Elpida Phithak, Martin Krusche, Olaf Penack, Tobias Alexander, Werner Stenzel, Manfred Wuhrer, Kamran Movassaghi, Thomas Dörner, Eicke Latz, Thomas Vogl, Antonia Busse, Georg Schett, Hans Ulrich Scherer, Rene E. M. Toes, Arnd Kleyer, Ulrich Keller, Lars Bullinger, David Simon, Gerhard Krönke. CD19 CAR T cell therapy for treatment-refractory seropositive rheumatoid arthritis: a phase 1 trial. Nature Medicine, 2026; DOI: 10.1038/s41591-026-04603-3

Courtesy:

Charité - Universitätsmedizin Berlin. "A cancer therapy put severe rheumatoid arthritis into remission." ScienceDaily. ScienceDaily, 29 August 2026. <www.sciencedaily.com/releases/2026/08/260828082330.htm>. 

 

 

 

 

 

Researchers unveil sustainable spirulina solution to vitamin B12 deficiency

Scientists have found a way to grow Spirulina that produces biologically active vitamin B12 at levels comparable to beef, potentially overcoming one of the biggest nutritional limitations of this widely promoted algae.

The research, published in the scientific journal Discover Food, was led by Dr. Asaf Tzachor, Founder and Academic Director of the Aviram Sustainability and Climate Program at Reichman University, together with researchers from Iceland, Denmark and Austria. Using advanced biotechnology and carefully controlled light conditions, the team produced carbon-neutral, nutrient-rich Spirulina biomass containing active vitamin B12. According to the researchers, this is the first time biologically active vitamin B12 has been reported in Spirulina.

A Global Vitamin B12 Problem

Vitamin B12 is an essential micronutrient involved in several critical processes in the body, including red blood cell formation and normal nervous system function. More than a billion people worldwide are estimated to have low levels of the vitamin.

For many people, meat and dairy products are important dietary sources of B12. The recommended intake cited by the researchers is 2.4 µg/day. However, producing animal-based foods at the scale required to meet global demand also carries environmental costs, which has driven interest in more sustainable alternatives.

Spirulina blue green algae (Arthrospira platensis) has often been promoted as one such option because it is nutrient dense and can be cultivated with a relatively small environmental footprint. But there has been a major obstacle.

Traditional Spirulina contains much of its B12 in the form of pseudo-vitamin B12. Although chemically similar to the vitamin humans need, this form is not bioavailable to people, meaning the body cannot effectively use it. That limitation has prevented conventional Spirulina from serving as a reliable replacement for animal-sourced vitamin B12.

Using Light to Change Spirulina's Nutrition

To address that problem, researchers from Reichman University, University of Natural Resources and Life Sciences, Vienna, Ruppin Academic Center, Danish Technological Institute, and MATIS, Iceland, carried out an exploratory study of a biotechnology platform developed by VAXA Technologies in Iceland.

The team examined the system's engineering design, its inputs (such as energy), and the nutritional composition of the biomass it produced.

A central feature of the technology is photonic management (modified light conditions). By changing the light environment in which Spirulina grows, the researchers were able to encourage production of biologically active vitamin B12.

The cultivated Spirulina also contained other bioactive compounds associated with antioxidant, anti-inflammatory, and immune-boosting properties.

Most notably, the resulting carbon-neutral biomass contained 1.64 µg of active vitamin B12 per 100 grams, compared with 0.7-1.5 μg per 100 grams in beef.

Dr. Asaf Tzachor explains, "the findings demonstrate that photosynthetically controlled Spirulina can produce desirable levels of active vitamin B12, offering a sustainable alternative to traditional animal-source foods."

Could Spirulina Supply Vitamin B12 at Scale?

The researchers also explored what could happen if the system were expanded far beyond its current scale.

In one scenario, reallocating electricity currently used by heavy industry in Iceland could support production of 277,950 tonnes of Spirulina biomass each year. The researchers estimate that this amount would contain about 4555 grams of active vitamin B12 annually.

According to their calculations, that quantity could provide the recommended dietary allowance (RDA) for more than 13.8 million children aged 1-3.

More ambitious production scenarios could potentially supply enough vitamin B12 to meet the RDA for more than 26.5 million children aged 1-3 and more than 50 million children aged 0-6 months.

These figures are projections based on possible scale-up scenarios rather than existing production levels, but they illustrate the nutritional potential the researchers see in the technology.

A More Sustainable Source of an Essential Vitamin

If the approach can be successfully expanded, photosynthetically controlled Spirulina could provide another route for addressing vitamin B12 deficiency while reducing some dependence on meat and dairy production.

The work also highlights how biotechnology can alter the nutritional properties of microorganisms and other rapidly growing food sources. Rather than simply cultivating conventional Spirulina, researchers are changing the conditions under which it grows to encourage production of specific compounds that are useful to humans.

The findings represent a step toward developing more sustainable sources of essential nutrients, although further research and larger-scale production will be needed to determine how the technology could fit into real-world food systems.

Reichman University and the Aviram Foundation established the Aviram Sustainability and Climate Program in response to growing environmental and public health challenges around the world. The program trains students from a range of disciplines to develop strategies for addressing resource scarcity, climate change, and extreme weather events, as well as food, water, and energy crises.

 

Journal Reference:

1. A. Tzachor, S. P. van den Oever, H. K. Mayer, M. Asfur, A. Smidt-Jensen, M. Geirsdóttir, S. Jensen, B. O. Smárason. Photonic management of Spirulina (Arthrospira platensis) in scalable photobioreactors to achieve biologically active unopposed vitamin B12. Discover Food, 2024; 4 (1) DOI: 10.1007/s44187-024-00152-1

Courtesy:

Reichman University. "Researchers unveil sustainable spirulina solution to vitamin B12 deficiency." ScienceDaily. ScienceDaily, 30 August 2026. <www.sciencedaily.com/releases/2026/08/260829035227.htm>. 

 

 

 

Widely prescribed blood pressure drugs linked to 33% higher kidney risk in type 2 diabetes

 

New findings presented at the 63rd ERA Congress suggest that a commonly prescribed group of blood pressure drugs may be linked to worse kidney outcomes in people with type 2 diabetes (T2D), including patients already taking newer medications designed to protect kidney function.

The medications, known as dihydropyridine calcium-channel blockers (DCCBs), lower blood pressure by relaxing blood vessels. They are often prescribed as second-line treatments for people with diabetic kidney disease (DKD). In the new study, patients who took DCCBs in addition to standard therapies experienced a significantly greater risk of major adverse kidney events than patients treated with other blood pressure medications.

Protecting the Kidneys in Type 2 Diabetes

DKD is among the most common causes of kidney failure worldwide. The condition develops as prolonged high blood sugar damages tiny blood vessels within the kidneys, gradually interfering with their ability to remove waste from the bloodstream. Keeping blood pressure under control is a key part of managing the disease because elevated blood pressure can speed up this damage.

Treatment for DKD has changed considerably in recent years with the introduction of two important classes of medication. Renin-angiotensin system (RAS) inhibitors lower blood pressure while also reducing pressure inside the kidney's filtering structures. Sodium-glucose cotransporter-2 (SGLT2) inhibitors were initially developed to treat diabetes, but they are now also recognized for their ability to protect kidney function and lower the risk of kidney failure. The two drug classes are now part of standard treatment for many people with DKD.

Study Tracks More Than 31,000 Patients

Researchers examined health data from 31,031 adults with T2D between 2016 and 2021. Every participant was receiving both RAS and SGLT2 inhibitors. Of the total group, 12,172 (39.2%) were also taking DCCBs, while 18,859 (60%) were being treated with other antihypertensive medications. The median follow-up period was approximately 3.5 years.

After accounting for differences in patients' initial clinical and demographic characteristics, the researchers found that DCCB use was associated with a 33% greater risk of a major adverse kidney event (R 1.33, 95%, CI 1.03-1.73).

Researchers classified these events as either a major loss of kidney filtration capacity, involving a decline of 40% or more in estimated glomerular filtration rate (eGFR), the standard measure of kidney function, or progression to end-stage kidney disease that required dialysis or transplantation.

"DCCBs are widely used as second-line blood pressure treatments in patients with DKD," said Dr. Timna Agur, lead author of the study. "Our findings raise important questions about whether these medications are always the best option for patients already receiving modern kidney-protective therapies."

Why DCCBs Could Affect Kidney Function

The researchers suggest that the association may be related to how DCCBs alter blood flow through the kidneys. In DKD, the kidneys are already dealing with elevated pressure and hyperfiltration, a condition in which their filtering structures are placed under excessive strain.

DCCBs may relax the blood vessels that carry blood into these filtering units more strongly than they affect the vessels carrying blood away. According to the researchers, this imbalance could increase pressure inside the filtering structures and potentially contribute to continued kidney damage.

"We initially thought the kidney-protective effects of SGLT2 inhibitors might counterbalance the potential harms associated with DCCBs," said Dr. Agur. "However, the increased risk of kidney disease progression appeared to persist even in this group."

More Research Is Needed

Because the study was observational, the researchers emphasize that it cannot show that DCCBs directly caused the poorer kidney outcomes. Still, they say the association deserves attention because these medications are so frequently prescribed to people with DKD.

"Further prospective studies and randomized controlled trials are needed to confirm these observations and better define the safest blood pressure treatment strategies for patients with DKD," concluded Dr. Agur. "However, given how commonly these medications are prescribed, any increase in kidney risk could have important implications for large numbers of patients with DKD."

Story Source:

Materials provided by European Renal Association (ERA). Note: Content may be edited for style and length.

 

Courtesy:

European Renal Association (ERA). "Widely prescribed blood pressure drugs linked to 33% higher kidney risk in type 2 diabetes." ScienceDaily. ScienceDaily, 18 August 2026. <www.sciencedaily.com/releases/2026/08/260816044844.htm>. 

 

 

 

 

Scientists turn probiotic bacteria into tiny drug factories for pancreatic cancer

Cancer immunotherapy has dramatically changed how doctors treat many forms of cancer, yet pancreatic cancer has remained particularly resistant to these advances. A major obstacle is the environment that develops around pancreatic tumors. These tumors often create a "cold" tumor microenvironment that blocks immune cells from launching an effective attack.

Researchers at the University of Chicago have now developed a new approach that could help overcome this problem. In a study published in Science Advances, the team used BifidoSumIL-2, an engineered strain of Bifidobacterium longum, a probiotic bacterium naturally found in the gut, to carry an immune-stimulating treatment directly into tumors.

In animal models, the therapy slowed the growth of pancreatic tumors by selectively activating T cells that fight cancer. Its effects became even stronger when researchers combined it with chemotherapy, radiotherapy or immunotherapy. The findings suggest that BifidoSumIL-2 could eventually provide a new way to improve how pancreatic tumors respond to treatment.

Using Bacteria to Deliver Cancer Therapy

"A big unmet medical need has been pancreatic cancer, and so that was going to be our mountain to climb," said Ralph Weichselbaum, MD, the Daniel K. Ludwig Distinguished Service Professor and Chair of Radiation and Cellular Oncology at the University of Chicago.

BifidoSumIL-2 was created to release a modified version of interleukin-2 (IL-2) once it reaches a tumor. IL-2 is a potent immune signaling molecule that activates T cells involved in attacking cancer. Conventional IL-2 treatment, however, can produce serious side effects and can also stimulate immune cells that actually weaken the antitumor response.

The researchers sought to avoid these problems by using SumIL-2, a modified form of IL-2 engineered to more precisely activate cancer-fighting T cells while reducing stimulation of regulatory T cells. They then placed SumIL-2 inside Bifidobacterium longum so that the therapeutic molecule could be concentrated within tumors instead of throughout the body.

Developing the treatment required scientists from several disciplines to work together, including specialists in microbiology, synthetic biology, oncology, and immunology.

"This was a highly interdisciplinary effort," said Mark Mimee, PhD, Assistant Professor of Microbiology at the University of Chicago. "We had to bring together people who understand bacteria, people who understand tumors, and people who understand the immune system to make something like this possible."

Why Bifidobacterium Can Target Tumors

Bifidobacterium offered the researchers an unusual advantage as a delivery system. The bacterium grows in anaerobic environments, meaning places with very little oxygen. Low oxygen levels are common inside many solid tumors, including pancreatic tumors, while healthy tissues generally contain more oxygen and are therefore less suitable for the bacteria.

"Bifidobacterium is an obligate anaerobe, so it doesn't grow in the presence of oxygen," Mimee said. When the bacteria are injected systemically, they are cleared from healthy tissues with abundant oxygen. Inside the low-oxygen regions of tumors, however, they can become active.

That preference allows the engineered bacteria to function as microscopic drug factories inside tumors. Once there, they produce SumIL-2 where the treatment is needed rather than broadly throughout the body. Researchers also noted that Bifidobacterium has shown a favorable safety profile in preclinical models and is already well known as a probiotic organism. It is commonly present in yogurt and is generally recognized as a safe, off-the-shelf probiotic.

Engineering the organism was not simple.

"Bifidobacterium is not the easiest organism to work with," Mimee said. "It's anaerobic, it grows slowly, and the genetic tools for manipulating it are much more limited compared to model bacteria like E. coli. A lot of the work was just figuring out how to reliably engineer it."

Stronger Results With Combination Treatments

Tests in animal models showed that BifidoSumIL-2 preferentially gathered inside tumors, stimulated immune activity, and slowed the growth of pancreatic cancer. It also changed the tumor microenvironment in a potentially beneficial way by increasing the activity of cancer-fighting CD8+ T cells.

The results improved further when BifidoSumIL-2 was paired with established cancer treatments. Combining the bacterial therapy with chemotherapy, radiation therapy, or anti-PD-L1 immunotherapy led to better tumor control and longer survival than the individual treatments achieved on their own.

"This combination potential is one of the study's most important findings; BifidoSumIL-2 not only works by itself -- it works with radiotherapy, chemotherapy, and immunotherapy," Weichselbaum said.

Despite the encouraging findings, BifidoSumIL-2 has not been tested in humans. Future research will need to examine its long-term safety, the possibility of effects outside the intended tumor, how long the immune response lasts, and whether the bacteria might eventually be given orally instead of through injection. The researchers also want to investigate whether the strategy can be combined with newer pancreatic cancer treatments, including KRAS inhibitors.

The Growing "Bugs as Drugs" Approach

The research adds to growing interest in a strategy known as "bugs as drugs." By engineering probiotic bacteria to seek out tumors and produce therapies directly inside them, scientists may be able to concentrate powerful immune treatments where they are most useful while reducing unwanted effects elsewhere in the body.

The study, "Engineered probiotic Bifidobacterium for tumor-targeted pancreatic cancer therapy" was supported by funds from the Ludwig Foundation and the National Institutes of Health.

Additional authors include Jaehyun Lee, Kaiting Yang, Christina Nowicki, Wei Liu, Emile Naccasha, and Hua Liang from the University of Chicago; Zhichen Sun from the University of Texas Southwestern, Dallas; and Yang-Xin Fu from Tsinghua University, Beijing, China.

UChicago Medicine and the Biological Sciences Division continue to be at the forefront of cancer care and research. In April 2027, UChicago Medicine will open the AbbVie Foundation Cancer Pavilion, Chicago's first freestanding cancer pavilion, to bring advanced diagnostics, innovative treatments, translational discoveries, and comprehensive support to patients and the community.

Journal Reference:

1. Jaehyun Lee, Kaiting Yang, Christina A. Nowicki, Wei Liu, Kangdi Li, Emile Naccasha, Zhichen Sun, Yang-Xin Fu, Hua Liang, Ralph R. Weichselbaum, Mark Mimee. Engineered probiotic Bifidobacterium for tumor-targeted pancreatic cancer therapy. Science Advances, 2026; 12 (30) DOI: 10.1126/sciadv.adz1388

Courtesy:

University of Chicago Medical Center. "Scientists turn probiotic bacteria into tiny drug factories for pancreatic cancer." ScienceDaily. ScienceDaily, 19 August 2026. <www.sciencedaily.com/releases/2026/08/260816044830.htm>.

 

 

 

 

 

 

Coffee drinkers have less fat, more muscle, and surprising hormone differences

Coffee is consumed around the world every day, and earlier research has associated coffee drinking with a reduced risk of conditions including type 2 diabetes and cardiovascular disease. Scientists still do not fully understand the biological processes that might explain those connections. Now, new research from Finland suggests that regular coffee consumption is associated with healthier body composition, favorable metabolic markers, and distinct patterns involving sex hormones in men and women.

Researchers at the University of Oulu analyzed information from 2,264 people who were 46 years old and taking part in the Northern Finland Birth Cohort 1966. The team investigated how participants' usual coffee intake related to circulating metabolites, indicators of cardiometabolic risk, and sex hormone levels.

Coffee Drinkers Had Less Fat and More Muscle

People who consumed more coffee tended to have lower levels of both total body fat and visceral fat, along with greater skeletal muscle mass. These differences appeared even though participants with higher and lower coffee intake had a similar body mass index (BMI).

Higher coffee consumption was also associated with lower circulating concentrations of branched-chain amino acids in both men and women. When chronically elevated, these biomarkers have previously been associated with insulin resistance and a greater risk of developing type 2 diabetes.

Coffee Intake Was Linked to Different Hormone Patterns

Some of the clearest differences appeared among men. Greater coffee consumption was associated with a more favorable glucose-insulin profile, higher levels of total and bioavailable testosterone, and greater concentrations of sex hormone-binding globulin (SHBG). However, free testosterone and the free androgen index were modestly lower.

The hormonal associations were less extensive in women. Higher coffee consumption was mainly associated with increased SHBG and lower measures of free androgens.

"Coffee is consumed by millions of people every day, yet we still know surprisingly little about how it relates to our metabolism and hormones. What stood out in our findings was a distinct hormonal signature that didn't disappear even after we took into account BMI and lifestyle factors, with several of these associations differing between men and women," says Luca Verroest, lead author of the study and Doctoral Researcher at the University of Oulu.

Hormones Could Offer a Clue to Coffee's Health Links

The findings raise the possibility that hormonal pathways could help explain some of the previously observed relationship between coffee consumption and metabolic health. Because the research was observational, however, it cannot establish that drinking coffee directly caused any of the biological differences identified in the study.

The setting also makes the research especially relevant. Finland ranks among the world's highest coffee-consuming countries, with average annual consumption of approximately 11.8 kilograms (26 pounds) per person.

Researchers say the results offer a starting point for studies designed to determine whether coffee itself produces these biological changes and, if so, which compounds may be responsible. Scientists are currently investigating these questions using animal models, with the longer-term aim of moving toward human intervention studies.

Additional research will be necessary before the findings can be used to shape dietary recommendations.

The study, "Associations of habitual coffee intake with testosterone and cardiometabolic markers: the Northern Finland Birth Cohort 1966 study," was published in the European Journal of Nutrition.

 

Journal Reference:

1. Luca Verroest, Jari Jokelainen, Shalini Choudhary, Jaroslaw Walkowiak, Toni Karhu, Saranya Palaniswamy, Juha Auvinen, Marjo-Riitta Jarvelin, Karl-Heinz Herzig, Ghulam Shere Raza. Associations of habitual coffee intake with testosterone and cardiometabolic markers: the Northern Finland birth cohort 1966 study. European Journal of Nutrition, 2026; 65 (5) DOI: 10.1007/s00394-026-04038-z

Courtesy:

University of Oulu, Finland. "Coffee drinkers have less fat, more muscle, and surprising hormone differences." ScienceDaily. ScienceDaily, 19 August 2026. <www.sciencedaily.com/releases/2026/08/260819041228.htm>. 

 

 

 

This ultrasound treatment may help stop arthritis before it starts

Researchers at The University of Alabama in Huntsville (UAH), part of The University of Alabama System, have identified a promising new use for continuous low-intensity ultrasound that could one day help treat joint injuries and reduce the risk of post-traumatic osteoarthritis. Their findings suggest the non-invasive approach may shift the body's immune response away from long-lasting inflammation and toward tissue repair, offering a potential drug-free strategy for improving healing.

The study, published in the Nature journal Scientific Reports, was led by Dr. Anuradha Subramanian, professor of chemical and materials engineering. It combined biological research conducted by Dr. Shahid Khan during his doctoral studies with computational and statistical analysis developed by Dr. Satyaki Roy, professor of mathematical sciences, along with contributions from graduate student Owen Trippany. The research was funded by the National Institutes of Health through an R01 grant awarded to Subramanian.

How Ultrasound Influences Immune Cells

The team focused on macrophages, specialized immune cells that play a key role in both inflammation and tissue repair, to understand how they respond to continuous low-intensity ultrasound.

"Following injury, the body recruits inflammatory 'defender' macrophages (M1) to clear damaged tissue and healer macrophages (M2) to support repair and recovery," Subramanian explains. "Persistent dominance of defender macrophages can create a prolonged inflammatory environment that contributes to post-traumatic osteoarthritis."

The researchers wanted to determine whether ultrasound could encourage these immune cells to transition from an inflammatory state to one that promotes healing.

"In an 'M1' state, microphages promote inflammation to fight damage or infection, but prolonged M1 activity can also harm healthy tissue," Subramanian notes. "In contrast, 'M2-like' macrophages support tissue repair and recovery. Shifting macrophages toward an M2-like state is important, because it may help reduce chronic inflammation while encouraging healing in damaged joints. Our findings suggest that continuous low-intensity ultrasound may help restore this balance by promoting a more reparative macrophage response."

Roy says chronic inflammation is a major factor in the development of post-traumatic osteoarthritis.

"Post-traumatic osteoarthritis is driven in part by persistent inflammation that limits tissue repair and accelerates joint degeneration," Roy adds. "Our team is interested in continuous low-intensity ultrasound because it offers a non-pharmacological, non-invasive approach that may help regulate immune cell behavior and promote a more reparative healing environment in injured joints."

A More Realistic Model of Joint Injury

To better recreate the conditions inside an injured joint, the researchers relied on fibronectin fragments, molecules generated as damaged tissue breaks down, instead of using only conventional laboratory methods to trigger inflammation. This approach produced a model that more closely reflects the biological environment that develops after a joint injury.

The team also combined transcriptomics, the large-scale study of gene activity, with an advanced computational method known as differential clustering. Rather than analyzing genes one by one, this technique identifies groups of genes whose behavior changes together, providing a broader picture of how immune cells respond to ultrasound treatment.

"This allowed us to study not only which genes changed, but also how groups of genes changed their coordinated behavior in response to ultrasound stimulation," Roy says.

Early Results Show Reduced Inflammation

The researchers found that continuous low-intensity ultrasound lowered biological markers linked to inflammation while increasing markers associated with a more reparative, M2-like macrophage state.

Although the research is still limited to laboratory experiments, the findings suggest that non-drug, non-invasive technologies could eventually be used to influence immune cell behavior and improve healing after joint injuries. The researchers believe the technique could become part of future treatments designed to slow the progression of osteoarthritis and improve recovery after joint trauma.

"The next steps will involve validating these findings in animal models of early post-traumatic osteoarthritis and studying how ultrasound-based modulation affects long-term tissue repair in joint injury settings," Subramanian says.

Journal Reference:

1. Shahid Khan, Owen Trippany, Anuradha Subramanian, Satyaki Roy. Continuous low-intensity ultrasound influences the transcriptomic profile in M1 macrophages by downregulating inflammation and promoting M2-like markers. Scientific Reports, 2026; DOI: 10.1038/s41598-026-53228-6

Courtesy:

The University of Alabama in Hunstville. "This ultrasound treatment may help stop arthritis before it starts." ScienceDaily. ScienceDaily, 12 July 2026. <www.sciencedaily.com/releases/2026/07/260710003521.htm>. 

 

 

Scientists finally crack nature's secret for building better cancer drugs

Scientists have uncovered how bacteria naturally manufacture multiple versions of powerful cancer drugs, solving a mystery that has puzzled researchers for decades. The discovery could help speed the development of new treatments for cancers that are still difficult to treat.

For years, scientists have hoped to harness bacterial enzymes to create new drug variants through a process known as combinatorial biosynthesis. However, progress has been limited because researchers did not fully understand how the enzymes coordinate their work.

Published in Nature Communications, the new study reveals how bacterial enzymes communicate with one another to assemble a family of closely related anti-cancer compounds. That family includes Romidepsin (Istodax), an FDA-approved treatment for certain blood cancers. By uncovering this natural "mix and match" system and reproducing its underlying principles in the laboratory, the researchers have established a new strategy for designing future cancer therapies.

"For decades, we've known that bacteria can naturally produce multiple versions of powerful anti-cancer drugs, yet we had no idea how they achieved this," said first author Dr. Munro Passmore, Research Fellow, Department of Chemistry, University of Warwick. "This work finally cracks that code. We've identified how the different enzymes communicate and cooperate to produce these drug variants, something that has eluded researchers because the system is so elegantly economical. It's the breakthrough we needed to actually engineer these drugs ourselves."

Tiny Molecular Connectors Reveal Nature's Drug-Making Strategy

The researchers discovered that small molecular regions known as 'docking domains' serve as connectors between the core drug-building machinery and the enzymes responsible for adding different components. These docking domains share a conserved connection point that allows them to interact with multiple enzyme partners.

This flexible design explains how bacteria can create a variety of related drug molecules while still maintaining the precision needed for the compounds to remain effective.

The study also sheds light on how these natural drug-producing systems evolved. According to the researchers, the newly identified compound most likely developed from a related drug-producing pathway through gene duplication and recombination over time.

Prof. Greg Challis, Monash Warwick Alliance Professor of Sustainable Chemistry, University of Warwick and Monash University concludes: "This research gives us a blueprint to do what nature does, but better and faster. By reverse-engineering nature's evolutionary logic, we can now design synthetic pathways that generate new anti-cancer drug candidates with properties optimized for clinical use, such as superior potency, improved selectivity, fewer side effects. Our immediate goal is to build an expanded library of candidates for various cancers where new treatments are urgently needed. This discovery is moving us from understanding how the systems work to building new ones."

How the Discovery Could Improve Cancer Drug Development

The work focuses on a class of anti-cancer medicines known as HDAC inhibitors. These drugs block histone deacetylases, enzymes that help regulate which genes are switched on or off inside cells. Romidepsin (Istodax) is an FDA-approved HDAC inhibitor used to treat T-cell lymphomas.

A chemically related compound called FR-901375 has been known for decades, but scientists had never identified the biological pathway bacteria use to produce it. This study finally fills in that missing piece.

Like other HDAC inhibitors in its family, FR-901375 belongs to a group of complex cyclic molecules called depsipeptides. These compounds are assembled from amino acid building blocks along with a conserved hydroxy acid pharmacophore, all connected through a combination of peptide and ester bonds.

Inside bacteria, these molecules are built by massive protein complexes called PKS-NRPS hybrids, which combine the activities of polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS). The new research shows that the key to this assembly process is the docking domains, which act like molecular connectors that allow one part of the production line to recognize and pass its product to the next. This mechanism is what enables combinatorial biosynthesis and allows bacteria to naturally generate multiple drug variants.

How the Researchers Solved the Mystery

To uncover how this system works, the team combined structural biology, biochemistry, genetics, and computational modeling.

Their work included:

• Bioinformatic searches of public databases that identified the FR-901375 biosynthetic gene cluster in Pseudomonas chlororaphis subsp. piscium, with the findings confirmed by mass spectrometry analysis of extracted metabolites.
• In vitro reconstitution experiments using purified protein domains that demonstrated productive enzyme-enzyme interactions, verified with intact protein mass spectrometry.
• AlphaFold computational modeling to predict protein complex structures, followed by carbene footprinting mass spectrometry to experimentally map the interaction sites.
• Site-directed mutagenesis experiments that confirmed the importance of the predicted binding residues.
• Gene deletion studies in bacterial strains showing that the docking domains are essential for the system to function in vivo.
• Comparative analysis of biosynthetic gene clusters from multiple HDAC inhibitor-producing bacteria, revealing evolutionarily conserved features shared across these natural drug-making systems.

Journal Reference:

1. Munro Passmore, Xinyun Jian, Xinyi Zhao, Emmanuel L. C. de los Santos, Douglas M. Roberts, Józef R. Lewandowski, Matthew Jenner, Lona M. Alkhalaf, Gregory L. Challis. Molecular basis for depsipeptide HDAC inhibitor combinatorial biosynthesis. Nature Communications, 2026; 17 (1) DOI: 10.1038/s41467-026-74383-4

Courtesy:

University of Warwick. "Scientists finally crack nature's secret for building better cancer drugs." ScienceDaily. ScienceDaily, 8 July 2026. <www.sciencedaily.com/releases/2026/07/260701205001.htm>.

 

 

 

Alzheimer's tau protein has a surprising secret role in memory

New research has revealed that tau, a protein best known for its connection to Alzheimer's disease, is also essential for creating long lasting memories. The discovery provides new insight into how healthy memory works and could help guide future efforts to develop treatments for dementia.

The study, led by Flinders University in partnership with researchers from the University of New South Wales and Macquarie University, was published in Nature Communications. It found that tau helps organize and stabilize memories so they can be retained over time.

The researchers studied "remote memory" in mice, which refers to memories recalled days or weeks after an experience. They discovered that tau is not necessary for learning something new or remembering it shortly afterward. Instead, it plays a crucial role in making those memories durable over the long term.

Because the research was conducted in mice, the findings cannot be directly applied to human memory or Alzheimer's disease. Even so, the results offer valuable clues that could shape future dementia research and treatment strategies.

Tau's Role in Long Lasting Memory

Senior author Associate Professor Arne Ittner, a neuroscientist from Flinders' College of Medicine and Public Health, says the findings help explain why people with dementia may still be able to learn new information initially, yet struggle to retain it.

"Why some memories last while others fade has long puzzled scientists and our study shows that tau plays a key role in how the brain forms long-lasting memories. Without it, memories can still form in the moment, but they are weaker," says Associate Professor Ittner.

The team focused on specialized brain cells called "engram cells," which create the physical record of a memory. When a new experience occurs, only a small number of these cells are selected to store it.

According to the study, tau is active during this critical stage of memory formation, helping determine exactly which engram cells are recruited to preserve the experience.

One of the study's lead authors, Renée Kosonen, says tau acts like an organizer that helps the brain build accurate and lasting memories.

"Our findings show that tau helps determine which cells are selected to store a memory, shaping how an experience forms a lasting memory trace," says Ms Kosonen, a researcher at Flinders' Neuroscience and Dementia Research.

How Tau Organizes Memory

The researchers also found that tau reduces unnecessary or "noise" activity in the brain during memory formation. By limiting this background activity, tau allows only a specific group of cells to become part of a memory, producing clearer and more stable memory traces.

The team identified an important molecular process behind this effect. As learning takes place, tau undergoes a subtle chemical change called phosphorylation, which helps coordinate the activity of engram cells.

Although abnormal tau phosphorylation is a well known feature of Alzheimer's disease, the study shows that controlled, low level phosphorylation is a normal and essential part of healthy brain function.

New Clues About Alzheimer's Disease

The researchers made another surprising discovery. Even in the absence of tau, memory traces still existed and could be recovered by directly stimulating engram cells. This suggests that tau is not required to store memories themselves. Instead, it appears to be needed to connect natural cues, such as sights and sounds, with the ability to recall those memories.

The findings also provide new insight into how Alzheimer's related tau may interfere with memory. When disease associated forms of tau were present in engram cells during learning, they disrupted the creation of new memories. When those abnormal forms appeared after memories had already formed, they interfered with the brain's ability to retrieve them.

These effects were associated with abnormal patterns of brain activity, suggesting that memory problems in dementia may result not only from memories being lost, but also from disruptions in how memories are organized and accessed.

"Knowing how tau supports the formation and recall of memory could help us better understand what goes wrong in memory loss," says Associate Professor Ittner.

"Future research will hopefully be able to confirm concepts developed in our study in human memory and show their implication in dementia."

The researchers conclude that tau should be viewed not only as a protein involved in Alzheimer's disease, but also as a fundamental regulator of how the brain organizes, stores, and retrieves lasting memories. That new perspective could deepen scientists' understanding of both healthy memory and the biological changes that contribute to Alzheimer's disease.

Journal Reference:

1. Renée Kosonen, Kristie Stefanoska, Yijun Lin, Samantha Edwards, Emmanuel Prikas, Josefine Bertz, Anne Poljak, Lars M. Ittner, Arne Ittner. Tau T205 phosphorylation modulates engram cell recruitment and remote memory in mice. Nature Communications, 2026; DOI: 10.1038/s41467-026-73207-9

Courtesy:

Flinders University. "Alzheimer's tau protein has a surprising secret role in memory." ScienceDaily. ScienceDaily, 12 July 2026. <www.sciencedaily.com/releases/2026/07/260710003535.htm>.  

 

 

 

Scientists may have finally found how Alzheimer's kills brain cells

Scientists have identified evidence of a previously unknown process that may explain how brain cells die in Alzheimer's disease and frontotemporal dementia (FTD). The discovery, centered on a mechanism known as karyoptosis, could point researchers toward new ways to slow the progression of these devastating conditions.

Many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and FTD, are marked by the buildup of harmful proteins inside neurons. Over time, these nerve cells die, contributing to memory loss and other symptoms. Although scientists have long known about several forms of cell death, including apoptosis, those mechanisms have never fully explained the extensive neuron loss seen in these disorders.

Now, researchers from King's College London, working with the UK Dementia Research Institute and supported in part by Alzheimer's Research UK, have identified karyoptosis as a potential missing link connecting toxic protein accumulation to the death of brain cells.

Karyoptosis refers to a series of chemical reactions set in motion when toxic proteins accumulate inside a cell. As the process unfolds, the cell's nucleus, which contains its genetic material, gradually shrivels before ultimately breaking apart.

Evidence Found in Alzheimer's and FTD Brains

The findings, published in Nature Communications, are based on an analysis of 3,000 brain cells collected from 28 people with either FTD or end stage Alzheimer's disease. Using computational algorithms, the researchers identified different forms of cell death occurring within the tissue.

They found signs of karyoptosis in 35 percent of cells from the frontal cortex of people with Alzheimer's disease, compared with just 15 percent of cells from healthy older adults.

"This study is the culmination of a 10-year journey at King's, from when we first identified karyoptosis in a relatively rare disease to discovering that it is a common feature of dementias which affect millions of people."

A Possible New Target for Dementia Treatments

The researchers also uncovered a key molecular pathway that appears to control karyoptosis. They found that forcing proteins inside neurons to clump together, a hallmark of many neurodegenerative diseases, can trigger this destructive process.

According to the study, the buildup of toxic proteins destabilizes the outer membrane of the nucleus, causing it to shrink and eventually disintegrate.

The team then investigated proteins known as kinases, which act as molecular switches in this pathway. In laboratory experiments using rat neurons, blocking these switches reduced markers associated with karyoptosis. In particular, the interaction between the kinase p38 MAP kinase and the protein LaminB1 emerged as a promising target for slowing or preventing the breakdown of the nucleus.

The researchers believe this pathway could eventually lead to therapies that reduce brain cell loss in dementia. Their next goal is to develop ways to selectively target the interaction between p38 MAP kinase and LaminB1 in humans.

"By specifically targeting the interaction between p38 MAP kinase and LaminB1 we may slow down the process of cell death, buying time for more pinpointed therapies against specific neurodegenerative diseases," said Dr. Manolis Fanto, Reader in Functional Genomics, Institute of Psychiatry, Psychology and Neuroscience, King's College London.

Building a Road Map for Future Therapies

"The death and loss of cells in the brain drives many symptoms experienced by people living with dementia. Our study uncovers a new series of chemical events which can coordinate cell death in brain cells. We have started to lay out the road map of how karyoptosis works, and I'm excited to see future breakthroughs this may drive in the dementia research community and beyond," said Dr. Rebecca Casterton, Senior Researcher at the UK Dementia Research Institute at King's and first author on the paper.

"For decades, we've known that toxic proteins build up in Alzheimer's disease and frontotemporal dementia, but exactly how they lead to the loss of brain cells has remained unclear.

"The identification of karyoptosis is a crucial step towards finding targets for treatments that could stop or slow cell loss. It could help widen the window for therapies that tackle the underlying causes of disease, bringing us closer to a cure for dementia. This is why Alzheimer's Research UK funds and supports research," said Dr. Sara Rodrigues, Senior Research Manager at Alzheimer's Research UK.

The study, "Karyoptosis mediates cell death and neurodegeneration upon proteotoxic stress," was published in Nature Communications.

The research was primarily funded by Alzheimer's Research UK and the Biotechnology and Biological Sciences Research Council International Partnership. Additional support came from a studentship provided by the UK Medical Research Council and the UK Dementia Research Institute.

Journal Reference:

1. Rebecca Casterton, Aitana Martinez-Cotrina, Jodi Barnard, Eleanor Wycherley, Yanling Hu, Rhys Anderson, Sebastien Janel, Jiin Byun, Olivia Houghton, Daniel A. Solomon, Juan Alcalde, Frank Lafont, Marc-David Ruepp, Frank Hirth, Bart Tummers, Yong-Yeon Cho, Gian De Nicola, Sarah Mizielinska, Manolis Fanto. Karyoptosis mediates cell death and neurodegeneration upon proteotoxic stress. Nature Communications, 2026; 17 (1) DOI: 10.1038/s41467-026-73802-w

Courtesy:

King's College London. "Scientists may have finally found how Alzheimer's kills brain cells." ScienceDaily. ScienceDaily, 5 July 2026. <www.sciencedaily.com/releases/2026/06/260626124701.htm>.

 

 

Streetlights are trapping thousands of pill bugs in giant “death spirals”

 

Researchers have uncovered a surprising side effect of artificial lighting: ordinary streetlights can lure thousands of tiny land dwelling isopods into giant synchronized "death spirals." The newly documented behavior, observed in Israel, is the first of its kind and suggests that human made lighting can dramatically disrupt the instincts of small ground dwelling animals.

The study was led by PhD student Idan Sheizaf under the supervision of Prof. Ariel Chipman at The Hebrew University of Jerusalem. Published in Ecology and Evolution, the research describes how land dwelling isopods, relatives of crabs and shrimp that are better known as woodlice or pill bugs, abandon their normally solitary habits to join enormous circular formations containing more than 5,000 individuals.

A surprising discovery in northern Israel

The unusual behavior first came to light after amateur naturalist Eviatar Itzkovich noticed huge swirling groups of isopods during summer nights in the Golan Heights.

The researchers focused on the species Armadillo sordidus, a little studied isopod that typically spends its time hidden beneath rocks and damp leaf litter, where moisture helps prevent it from drying out.

Although woodlice commonly cluster together to conserve moisture, scientists had never documented coordinated movement on this scale. Before this work, very little was known about A. sordidus. The study also expanded the species' known range. Previously, it had only been recorded in southern Syria and the Golan Heights. Researchers have now documented it in the Jezreel Valley for the first time.

Experiments reveal the role of artificial light

To determine what was causing the strange circular marches, the team tested several possible explanations, including magnetic fields and different types of lighting.

Strong magnets placed near the moving isopods had no effect, even though the Golan Heights is known for unusual magnetic properties. The animals continued circling uninterrupted.

Ultraviolet flashlights attracted only a small number of isopods and never triggered the swirling formations.

White light, however, consistently produced the dramatic behavior. When researchers positioned a white lamp so that its beam shone straight down, the isopods repeatedly gathered into large rotating circles.

The experiments showed that the shape of the illuminated area is what matters most. A vertical beam creates a circular boundary of light on the ground. Drawn toward that edge, the isopods begin walking along its perimeter. As more individuals join, the movement reaches a tipping point and develops into a large, self sustaining circular procession.

Reflecting on the findings, Idan Sheizaf said: "While collective movement is common in the animal kingdom, seeing it in this form in isopods was entirely unexpected. It appears that the geometry of our modern world -- specifically the circular pools of light created by streetlights, is interacting with the natural instincts of these creatures to create a mesmerizing, yet potentially harmful, emergent phenomenon."

Why the "death spirals" may be dangerous

Although the swirling formations are visually striking, researchers believe they represent an unintended trap created by artificial light at night (ALAN), not a natural social behavior.

Most of the participants were female, and many were carrying eggs, making it unlikely that the gatherings were related to mating. Instead, the evidence suggests that artificial lighting is disrupting the animals' normal instincts.

The consequences could be severe. During one observation, a centipede preyed on the distracted isopods while they remained caught in the swirling formation. By pulling these animals out of their sheltered habitats and keeping them moving in circles, streetlights may leave them vulnerable to predators while also wasting energy needed for survival.

The findings highlight how even a simple change to the environment, such as installing a streetlight, can reshape ancient behaviors in small animals that often go unnoticed.

Journal Reference:

1. Idan Sheizaf, Eviatar Itzkovich, Ariel D. Chipman. A Novel Light‐Induced Collective Circular Movement in Armadillo sordidus Isopods. Ecology and Evolution, 2026; 16 (4) DOI: 10.1002/ece3.73487

Courtesy:

 The Hebrew University of Jerusalem. "Streetlights are trapping thousands of pill bugs in giant “death spirals”." ScienceDaily. ScienceDaily, 6 July 2026. <www.sciencedaily.com/releases/2026/06/260626125707.htm>. 

Scientists solve a 30-year rye pollen mystery that could transform cancer research

 

Nearly 30 years ago, researchers discovered two unusual molecules in rye pollen that appeared to slow tumor growth in animal studies. Despite the promising findings, the research reached a dead end because scientists could not determine the molecules' exact three dimensional structures.

Now, chemists at Northwestern University have solved that long standing mystery. By constructing the molecules from scratch in the laboratory, they confirmed the precise structures of secalosides A and B for the first time.

With an accurate molecular blueprint available, researchers can now investigate how these compounds from rye pollen, which comes from a cereal crop widely grown for its grain, interact with the immune system. That knowledge could eventually help guide the development of new approaches to cancer treatment.

The findings were published in the Journal of the American Chemical Society.

"In preliminary studies, other researchers found that rye pollen could help different animal models clear tumors through some unknown, non-toxic mechanism," said Northwestern's Karl A. Scheidt, who led the study. "Now that we confirmed the structure of these molecules, we can find the active ingredient -- or what part of the molecule is doing the work. This is an exciting starting point to make better versions of these molecules that could possibly inform approaches to cancer therapy."

Scheidt is a professor of chemistry at Northwestern's Weinberg College of Arts and Sciences and a professor of pharmacology (by courtesy) at Northwestern University Feinberg School of Medicine. He also is a member of the Chemistry of Life Processes Institute and of the Robert H. Lurie Comprehensive Cancer Center of Northwestern University.

Nature's Role in Drug Discovery

Many important medicines have their roots in nature. Scientists have long studied plants, fungi, and microbes for compounds that can inspire new treatments.

Morphine, a powerful pain medication, comes from the opium poppy. Taxol, an important chemotherapy drug, was first isolated from the Pacific yew tree. Statins, which help lower cholesterol and reduce the risk of heart disease, originated from fungi.

"Natural products aren't necessarily effective drugs on their own, but they are great leads," Scheidt said. "We can find inspiration in natural products and use chemistry to make better versions that are orally available, survive the metabolism and hit the right targets."

Rye pollen could eventually join that list. Rye pollen extract is already sold as a dietary supplement that many people use to support prostate health. However, scientists have not yet developed it into a pharmaceutical treatment. A major obstacle was the lack of a clear picture of the molecules' three dimensional structures.

Solving a Decades Long Molecular Puzzle

Traditional techniques, including advanced nuclear magnetic resonance spectroscopy, could not fully determine how key parts of the molecules were arranged. As a result, scientists spent decades debating between two possible structural models.

Both versions contained the same atoms connected in the same way and shared the same overall shape. The difference was that one critical region existed as a mirror image in each model. Even that subtle variation can dramatically affect how a molecule interacts with biological targets and whether it produces a biological effect.

"It's like your hands," Scheidt said. "They are mirror images of each other, but you need a different glove for each. If you had two left-handed gloves, it wouldn't work because your hands can't be superimposed on top of one another."

Building the Molecules From Scratch

To resolve the uncertainty, the Northwestern team relied on total synthesis, a process in which researchers build a natural molecule step by step in the laboratory.

The work proved exceptionally difficult because secalosides A and B contain an extremely rare, highly strained 10 membered ring at their core. That tightly compressed structure is notoriously challenging to assemble.

The researchers overcame the problem by first creating a larger, more flexible ring. They then triggered a chemical reaction that converted it into the smaller strained ring in a single step.

After producing both proposed versions of the molecules, the team compared them with samples extracted from rye pollen. Only one matched perfectly, allowing the researchers to definitively identify the correct structures.

"We've demonstrated we can make the core of this natural product," Scheidt said. "Now, we're trying to find potential collaborators in immunology who could help us translate this to a possible clinical endpoint."

The study, "Synthesis and structural confirmation of secalosides A and B," was supported by the National Institute of General Medical Science, the Chemistry of Life Processes Institute Lambert Fellowship and the National Science Foundation.

Journal Reference:

1. Yunchan Nam, Anthony T. Tam, Troy E. Reynolds, Diego N. Rojas, Jonathan A. Brekan, Sneha Sil, Karl A. Scheidt. Synthesis and Structural Confirmation of Secalosides A and B. Journal of the American Chemical Society, 2025; 148 (1): 86 DOI: 10.1021/jacs.5c18864

Courtesy:

 Northwestern University. "Scientists solve a 30-year rye pollen mystery that could transform cancer research." ScienceDaily. ScienceDaily, 6 July 2026. <www.sciencedaily.com/releases/2026/06/260625014838.htm>. 

Scientists discover a completely different way to fight viruses

 

Scientists have uncovered a previously unknown way that sea anemones defend themselves against viruses, revealing that the evolution of animal immune systems may be far more diverse than previously believed. The newly identified defense relies on a protein that closely resembles one of the most important antiviral proteins in humans, yet performs the opposite function while still being essential for protecting the animal from infection. The findings suggest that evolution produced more than one successful strategy for fighting viruses across the animal kingdom.

The research, led by PhD candidate Ton Sharoni and Prof. Yehu Moran at the Hebrew University of Jerusalem in collaboration with scientists from the University of North Carolina at Charlotte, was published in Nature Ecology & Evolution. It challenges the long standing idea that animals inherited a single core antiviral system from a common ancestor and instead points to multiple evolutionary solutions for resisting viral infections.

An Ancient Animal Offers New Clues About Immunity

Viruses have threatened living organisms throughout evolutionary history. In humans and other vertebrates, one of the body's key antiviral defenses depends on a protein called MAVS. When a virus is detected, MAVS helps trigger the immune system so it can respond to the infection.

To investigate how old this defense system might be, the researchers studied sea anemones. These ancient marine animals split from the evolutionary line that eventually led to humans more than 600 million years ago. Because they are close relatives of corals and jellyfish, sea anemones provide scientists with a valuable glimpse into the early evolution of animal immunity.

During the study, the team discovered a previously unknown protein they named CARDIB (CARD Inhibitor Binding protein). At first, CARDIB looked remarkably similar to MAVS, leading researchers to believe it might perform the same antiviral role found in humans.

That assumption quickly fell apart.

"Everything about CARDIB suggested it should function like MAVS," said Prof. Yehu Moran, head of the Department of Ecology, Evolution and Behavior at the Hebrew University. "Instead, we discovered that it does the exact opposite. Rather than activating antiviral defenses, CARDIB normally suppresses them."

A Surprising Protein That Protects by Slowing the Immune System

The discovery immediately raised an important question. Why would an animal deliberately suppress its own immune response?

To find out, the researchers used CRISPR gene editing to remove the CARDIB gene from sea anemones before exposing them to viruses.

The results were unexpected. Sea anemones without CARDIB became much more susceptible to infection. Viruses multiplied more rapidly, the animals failed to properly activate their antiviral defenses, and their ability to fight infection dropped dramatically.

"The results were completely counterintuitive," said Sharoni. "Although CARDIB acts as a brake on the immune system under normal conditions, that brake turns out to be essential for mounting an effective antiviral response."

Overall, the experiments showed that sea anemones rely on an antiviral pathway that is fundamentally different from the one used by humans, even though both systems contain molecular components that look strikingly alike.

Natural Environment Confirms the Discovery

The researchers also wanted to determine whether this newly identified immune pathway mattered outside carefully controlled laboratory conditions.

To answer that question, genetically modified sea anemones were moved from laboratory aquaria into outdoor marine mesocosms supplied with natural estuarine water in South Carolina. This exposed the animals to the wide variety of viruses and microorganisms found in their normal environment.

The difference became obvious within days. Sea anemones lacking CARDIB and related antiviral genes accumulated substantially more viruses than unmodified animals. Researchers also found that one immune gene that appeared only moderately important in laboratory tests became clearly important under natural environmental conditions.

"This demonstrated that the pathway we discovered is not simply a laboratory phenomenon," said Moran. "It plays a crucial role in helping these animals cope with the viral challenges they face in nature."

Multiple Evolutionary Solutions to Fighting Viruses

The findings suggest that evolution did not settle on a single universal antiviral strategy. Instead, different groups of animals may have independently developed distinct molecular systems for detecting viruses and preventing them from spreading.

"Humans and sea anemones both need protection from viruses, but this work shows that evolution can organize those defenses in fundamentally different ways," Moran added.

The research also underscores the importance of looking beyond traditional laboratory animals. Ancient organisms such as sea anemones can preserve evolutionary innovations that would remain hidden if scientists focused only on humans, mice, and other commonly studied species.

As researchers continue exploring the remarkable diversity of life, discoveries like this are revealing that evolution has repeatedly found unexpected ways to solve some of biology's most fundamental challenges.

Journal Reference:

1. Ton Sharoni, Adrian Jaimes-Becerra, Sydney Birch, Hee-Jin Kwak, Daria Aleshkina, Magda Lewandowska, Joachim M. Surm, Hannah Justin, Reuven Aharoni, Adam M. Reitzel, Yehu Moran. An ancient anthozoan protein reveals an alternative evolutionary path of antiviral signalling. Nature Ecology, 2026; DOI: 10.1038/s41559-026-03112-3

Courtesy:

The Hebrew University of Jerusalem. "Scientists discover a completely different way to fight viruses." ScienceDaily. ScienceDaily, 30 June 2026. <www.sciencedaily.com/releases/2026/06/260630020534.htm>.