Friday, October 09, 2026

 

Your favorite music could help reduce the pain of small medical procedures



Scientists find that playing patients’ favorite music during a cannulation minimizes pain




Frontiers






If you hate needles, music might make you feel better during a cannula insertion… but it has to be the right kind of music. Although different musical interventions have repeatedly been reported to help with pain and stress, the evidence varies widely for different types of music and it’s hard to figure out what works best. To investigate, scientists played different kinds of music for patients about to undergo an intravenous cannula before an MRI — either Mozart, relaxation music, or the patients’ own favorite tunes. They found that playing patients’ favorite music worked best.  

“Although a needle puncture is a minor procedure, the level of pain can vary significantly from person to person,” said Dr Andrei Cristinel Dragnea of University Hospital Zürich, lead author of the article in Frontiers in Pain Research. “In modern medicine, the goal of treating physicians is not only to provide a successful diagnosis and therapy, but also to ensure that the procedure causes as little discomfort as possible.” 

“I would recommend listening to music to patients, especially patients who like music in general,” said Dr Meritxell Garcia Alzamora of University Hospital Zürich, senior author of the article. “In view of our results we will increase the application of music in venous punctures performed for radiological procedures, especially in anxious or claustrophobic patients.” 

Sweet music? 

The scientists recruited 204 patients undergoing a non-emergency MRI of the brain, spine, or head and neck. These patients’ procedures called for a contrast agent inserted into their veins with a cannula, which can hurt. A quarter of them acted as a control group, meaning they listened to no music, while three other groups listened to either their favorite music, music specifically designed for relaxation, or a piece of Mozart, Sonata KV448, which several studies have found to have therapeutic properties.  

Before the procedure started, patients assigned to the ‘favorite music’ group were asked to name an artist or song they would like to hear, and all patients were shown a visual scale that describes pain from a level of one (no pain) to 10 (worst pain of their life). This allowed the researchers to ask patients to rate their pain before and during the procedure, and then at two points afterwards — 30 seconds and two minutes later.  

“From the four conditions we examined, only favorite music and Mozart showed a positive effect,” said Garcia Alzamora. “Favorite music manifested a significant pain reduction effect both in patients with and without baseline pain — i.e. with preexisting pain before needle puncture. Mozart only showed significant pain relief in patients with preexisting pain.”  

Patients who were listening to their favorite music experienced less pain both 30 seconds and two minutes after the cannula was inserted. In a subgroup of patients who reported preexisting pain before cannulation, listening to their favorite music also reduced pain at the time of needle insertion, and listening to Mozart reduced pain two minutes after needle insertion.  

Pain levels seemed to improve more two minutes after cannulation than at the earlier time points, although this data can’t explain why. It could be that the initial discomfort of the cannula pulled people’s attention from the music, or that the mechanisms which make music helpful for pain reduction need some time to kick in.  

Relaxation music doesn’t soothe 

However, Mozart only seemed to work for the patients who reported being in pain before the cannulation, and the patients who listened to relaxation music or no music didn’t experience any change in their pain. 

“Relaxation music is usually characterized by a slow speed and low volume, and does not show noticeable dynamics,” said Garcia Alzamora. “These characteristics may have contributed to the patients disregarding relaxation music, which would explain the lack of pain relief.” 

“The intervention — in this case the venous puncture — consisted only of a very short-term pain with a small needle, although this can be very painful for some patients,” cautioned Dragnea, adding that it would be worth evaluating the benefits of music for patients undergoing procedures that are more painful and last longer. “Additionally, a technician accompanying and talking to the patient could be regarded as a confounder, as the mere presence of a person talking to you may be perceived as calming and distracting. However, all patients were exposed to the same conditions, so this confounder should not be over-interpreted.” 

 

Ingenious ‘molecular movie’ finally reveals how penicillin is made




University of Oxford
Animated molecular movie of penicillin biosynthesis

video: 

Animated molecular movie of penicillin biosynthesis. Each frame shows a different stage of the reaction as IPNS converts its substrate into penicillin. The animation was reconstructed from several time-resolved X-ray crystal structures collected at different reaction times, allowing the complete catalytic process to be visualized at atomic resolution.
Image credit: Patrick Rabe/University of Oxford and Greg Stewart/SLAC National Accelerator Laboratory.

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Credit: Patrick Rabe/University of Oxford and Greg Stewart/SLAC National Accelerator Laboratory.





Researchers from the University of Oxford and international collaborators have revealed previously unseen rapid chemical stages in the formation of β-lactam antibiotics like penicillin, offering insights that can support future antibiotic development. The findings have been published today (9 Oct) in Nature Catalysis.

Ever since penicillin was developed into a working drug at the University of Oxford in the early 1940’s, β-lactam antibiotics have been among the most important medicines for treating bacterial infection. Their activity depends on a special ring - the β-lactam ring - a highly strained chemical ring system that interferes with bacterial cell wall synthesis, ultimately causing the cell wall to fail and the bacteria to die.

Scientists have been studying how nature constructs this β-lactam ring for decades, but the key fleeting reaction intermediates have been too difficult to observe directly.

Rising rates of antimicrobial resistance- a process in which bacteria, fungi and other microorganisms evolve to survive the medicines designed to kill them, are undermining the effectiveness of existing antibiotics. With too few new antibiotics in development, understanding how nature builds these molecules is an important step towards replenishing the antibiotic pipeline.

In the new study, researchers from the University of Oxford in collaboration with partners from Diamond Light Source, Lawrence Berkeley National Laboratory, PAL-XFEL and SLAC National Accelerator Laboratory have used X-ray free-electron lasers to observe the enzyme isopenicillin N synthase, or IPNS as it converts its linear peptide substrate into the ring system of penicillin.

The new study shows, in unprecedented detail, how the enzyme IPNS achieves an exceptionally complex transformation in a single step. This resolves a long-standing mechanistic question that has remained unanswered for more than four decades.

Rather than relying on static X-ray crystallographic structures of the enzyme, the researchers followed the reaction in real time using ultrafast X-ray free-electron laser (XFEL) experiments.

The team captured several rapid stages in the reaction. These included a thioaldehyde intermediate formed just before the β-lactam ring is created, and a monocyclic β-lactam intermediate, representing the first ring-shaped structure on the way to forming the complete penicillin scaffold. These steps provide the clearest picture yet of how the IPNS enzyme assembles the penicillin scaffold.

The work also showed that water molecules inside the enzyme play a key role in guiding the reaction. Subtle movements throughout the enzyme help guide these chemical steps, showing that both the enzyme's shape and its chemistry work together to control penicillin formation.

To capture the reaction in real time, the researchers used a system in which thousands of tiny droplets containing anaerobic enzyme microcrystals were deposited onto a moving 2 mm wide tape. As the tape entered an oxygen filled chamber, oxygen rapidly diffused into the crystals and initiated the reaction simultaneously across the sample. By precisely controlling the speed of the tape, the researchers could determine how long each crystal reacted before reaching the X-ray interaction point, where an ultrafast XFEL pulse recorded an atomic resolution snapshot.

Combining thousands of these snapshots allowed the team to build a frame-by-frame “molecular movie” of penicillin biosynthesis. This method allows individual reaction intermediates that exist only for tiny fractions of a second to be observed at atomic resolution, and under physiological temperature and pressure, before they disappear.

Oxford has played a central role in the history of penicillin since the pioneering work of Nobel prize-winning scientists Prof Howard Florey and Sir Ernst Chain, and colleagues, who developed penicillin into the first clinically useful antibiotic during the Second World War. This new study ultimately builds on the work of Nobel prize-winning Oxford chemist Dorothy Hodgkin, who first solved the structure of penicillin in 1945 using X-ray crystallography.

Beyond penicillin, IPNS belongs to a large family of iron-dependent oxygenase enzymes involved in human biology, including ones that enable us to sense and respond to changes in oxygen availability. The mechanistic insights from this work therefore have implications far beyond antibiotics, offering new principles for enzyme engineering and catalyst design.

Professor Christopher Schofield, Professor of Chemistry, University of Oxford, and a senior author of the paper, said, “Penicillin has shaped modern medicine, but there is still much to learn about how nature builds this important antibiotic structure. By capturing these fleeting steps, we can better understand how enzymes control complex chemistry with remarkable precision.

“As rates of antimicrobial resistance continue to rise, understanding this process will ultimately help us make existing antibiotics more efficient and design new antibiotic structures.”

Today, one in six bacterial infections is resistant to antibiotics. Rising resistance threatens decades of progress in cancer care, transplant surgery and other areas of modern medicine, while also placing pressure on economies, health systems and food production.

Dr Patrick Rabe, Wellcome Career Development Award Investigator, University of Oxford and first author on the paper said, “These insights matter because they can inform how we think about antibiotic biosynthesis and future strategies for developing antibacterial medicines. The ability to capture structural snapshots over milliseconds to seconds of reaction time allows us to connect enzyme motion, iron chemistry and water-mediated proton transfer. This gives us a much richer view of how IPNS controls a difficult chemical transformation. By understanding this process in atomic detail, we can begin to think about engineering these enzymes to produce new or improved antibiotic scaffolds.”

This study brought together expertise in structural biology, spectroscopy, chemistry, computation and enzyme engineering. This approach provides a powerful way to study fleeting chemical intermediates that have previously been inaccessible, both in antibiotic biosynthesis and in other biologically important enzyme reactions.

Dr Allen M Orville, group leader of the XFEL Hub and co-author of the paper, said: “The XFEL Hub at Diamond brought specialist expertise in time-resolved X-ray methods and XFEL-based structural biology to this study. Working closely with our colleagues in Oxford and at partner facilities, we helped bring together the experimental approaches needed to capture these fleeting stages of enzyme catalysis. The results show the power of combining complementary expertise and X-ray techniques to move beyond static structures and reveal how enzymes work in real time. It is a great example of how time-resolved structural biology can uncover new principles of enzyme function and, ultimately, inform the design of new catalysts and therapeutics.” 

Notes for editors

For media enquiries and interview requests, contact Avni Gupta avni.gupta@chem.ox.ac.uk

The study 'Unanticipated intermediates during isopenicillin N synthase catalysis identified by time-resolved X-ray free-electron laser studies' will be published in Nature Catalysis at 10 AM BST / 5 AM ET Friday 9 October 2026 at https://www.nature.com/articles/s41929-026-01618-4 To view a copy of the study before this under embargo, contact Avni Gupta avni.gupta@chem.ox.ac.uk.

The work was led by researchers in the Department of Chemistry, University of Oxford, in collaboration with Lawrence Berkeley National Laboratory, SLAC National Accelerator Laboratory and international partners.

Experiments were carried out using X-ray free-electron lasers at LCLS (USA), PAL-XFEL (Republic of Korea), SACLA (Japan) and Diamond Light Source (UK).

About the University of Oxford

Oxford University has been placed number 1 in the Times Higher Education World University Rankings for the tenth year running, and number 3 in the QS World Rankings 2024. At the heart of this success are the twin-pillars of our ground-breaking research and innovation and our distinctive educational offer.

Oxford is world-famous for research and teaching excellence and home to some of the most talented people from across the globe. Our work helps the lives of millions, solving real-world problems through a huge network of partnerships and collaborations. The breadth and interdisciplinary nature of our research alongside our personalised approach to teaching sparks imaginative and inventive insights and solutions.

Through its research commercialisation arm, Oxford University Innovation, Oxford is the highest university patent filer in the UK and is ranked first in the UK for university spinouts, having created more than 300 new companies since 1988. Over a third of these companies have been created in the past five years. The university is a catalyst for prosperity in Oxfordshire and the United Kingdom, contributing around £16.9 billion to the UK economy in 2021/22, and supports more than 90,400 full time jobs.

About Diamond Light Source

Diamond Light Source is the UK’s national synchrotron serving scientists and researchers from around the world. It is a not-for-profit joint venture funded by UK Research & Innovation (UKRI) and Wellcome. Diamond provides academic and industry researchers access to facilities that enable world-changing science. The machine generates extremely bright light that is directed into laboratories known as beamlines. Scientists use the light to find solutions to humanity’s most critical challenges, from health, food security and biotechnology to energy, climate change and advanced materials. Diamond is in the process of upgrading to a fourth-generation synchrotron, generating a brighter and more coherent light. This will provide enhanced imaging and analysis capabilities, helping the UK to remain at the forefront of scientific discovery.

 

Fish may look fine in urban waters but their genes tell a different story


Blue damselfish remain abundant along Okinawa’s urbanized coasts, but gene activity reveals physiological stress that conventional environmental monitoring may miss.




Okinawa Institute of Science and Technology (OIST) Graduate University

Juvenile blue damselfish

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Tiny juvenile blue damselfish shelter in coral branches.

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Credit: Emma Gairin





Blue damselfish, with their striking blue hue, are easy to spot, even along Okinawa’s heavily urbanized coastlines. But while abundant, their gene activity reveals a hidden cost to living in human-impacted environments. 

A new Nature Communications study shows that fish living close to human activity can be well fed while simultaneously displaying molecular signs of chronic physiological stress, suggesting a possible “junk food effect.” The research, conducted by scientists at the Okinawa Institute of Science and Technology (OIST), the French National Centre for Scientific Research (CNRS), and the Indiana University School of Medicine, also opens the possibility of using organisms themselves as recorders of environmental conditions, with genome-wide gene activity revealing ecological impacts invisible to conventional environmental monitoring.

Coastal environments worldwide are increasingly under pressure from urbanization, including agricultural, industrial, and residential activity. In Okinawa, less than 40% of the coastline remains natural and unaltered. This is particularly relevant for young coral reef fish, which spend their early lives in calm, shallow waters close to shore. These nursery areas provide relatively safe conditions and abundant food, but their proximity to land also exposes young fish to the impacts of human activity. However, how these conditions affect fish during this important stage of their lives, and into adulthood, remains poorly understood — until now.

“Classic methods of ecological and environmental monitoring involve water sampling, or counting the number of fish species, but this doesn’t really tell us about the health of the fish,” explains first author Emma Gairin, research fellow and former PhD student in the Marine Eco-Eco-Devo Unit at OIST. “To know what the fish is experiencing, looking at gene activity is key.”

But this is easier said than done. For wild animals in the field, scientists have typically focused on the activity of just a few genes at a time. Yet many different factors can affect gene activity, such as temperature and salinity, making it difficult to tell whether differences in gene activity between fish from different environments are really associated with human activity.

Gairin continues: “Our approach was to look at the activity of all genes, not just a few, from fish across multiple different sites to see if we can distinguish any clear environmental signatures.”

The researchers collected blue damselfish (Chrysiptera cyanea), from 18 different sites across Okinawa’s main island, with varying levels of urbanization, ranging from almost pristine reefs in northern Okinawa, to heavily urbanized coastlines in the island’s south.

“Some of the sites we were sampling were really dirty and polluted, but still, there they were,” says Gairin. “But just because they are present, it doesn’t mean that they’re not under stress.

When they analyzed the gene activity of these fish, they found, surprisingly, that many of the genes traditionally used as markers of pollution failed to track urbanization. Their activity was often better explained by factors such as temperature or nutritional status. Only when the researchers looked at gene activity across the genome as a whole did the signature of human activity clearly emerge.

The researchers identified 425 genes in juveniles and 585 genes in adult livers whose activity was associated with urbanization, but not with any of the other environmental factors they measured. These included genes involved in inflammation and immune responses, which were more active in fish from urbanized areas.

The researchers then compared the wild fish with fish raised in the laboratory under different feeding conditions. Adult fish from urbanized areas showed gene activity patterns similar to those of well-fed laboratory fish. Yet these same urban fish also showed increased immune and inflammatory responses, revealing a striking trade-off between nutritional status and physiological stress.

These findings may help answer a long-debated question: why do young reef fish settle in highly urbanized, sometimes visibly degraded coastal areas when cleaner, more natural habitats are available nearby? One possibility is that these environments may be enriched with organic matter, making food abundant and easily accessible.

“We suggest this is a ‘junk food effect’. It’s like teenagers going to a fast food chain: there is plenty to eat, it is cheap, but it may not be good for their health!” says Professor Vincent Laudet, head of OIST’s Marine Eco-Evo-Devo Unit and senior author of the study. “For young fish, an urbanized coastal environment may offer a similar trade-off. There’s plenty of food, but at a physiological cost.”

Overall, the study reveals the potential of using gene activity to better understand environmental conditions and how urbanization affects the organisms living there.

“What is exciting here is that instead of simply measuring the environment around an animal, we can ask the animal itself what it has experienced,” concludes Laudet. “Genome-wide gene activity integrates the many different environmental influences acting on an organism and can reveal physiological effects that remain invisible when we measure water quality or simply count which species are present. And there is no reason why this approach should be limited to fish or coral reefs. In principle, any animal, in any ecosystem, could become a living sensor of environmental change.”

 

CTHULHU STUDIES

3D structure of DNA may explain how cephalopods evolved complex brains



Study suggests that the 3D "entanglement" of DNA may help drive evolutionary innovation




University of Vienna

Californian two-spot octopus (Octopus bimaculoides). Embryo at the final stage before hatching. The species is named after the two prominent blue eyespots that can help deter predators.

image: 

Californian two-spot octopus (Octopus bimaculoides). Embryo at the final stage before hatching. The species is named after the two prominent blue eyespots that can help deter predators.

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Credit: Natalie Grace Schulz





Octopuses, squid and cuttlefish, collectively known as coleoid cephalopods, have evolved exceptionally large and elaborately structured nervous systems capable of complex behaviours such as problem-solving and rapid camouflage. A new study by scientists at The University of Vienna suggests that the origins of this complexity may lie not just in the genes themselves, but in how the genome is organised in 3D. The researchers found that ancient, extensive reorganisation of the genome altered how DNA is arranged inside the cell. These shifts brought previously distant regions of DNA into contact, changing the way genes are regulated. Understanding this process could change how we think about how new traits emerge during evolution. The findings are currently published in the renowned journal Nature Communications. 

The team studied the 3D structure of the genome across octopus, squid and cuttlefish, combining data on DNA structure with gene activity. "The genome isn't just a sequence of genes. It's folded into a complex three-dimensional structure," said lead author Dr Thea Rogers. "Understanding how that structure evolves is becoming increasingly important for understanding how new forms of biological complexity arise."

"Regulatory entanglement" as a consequence of genome reorganisation

In cephalopods, a large-scale burst of genome reorganisation, which occurred hundreds of millions of years ago, dramatically reshuffled the genome and brought previously distant regions of chromosomes into close proximity.

The researchers found that when regions of DNA are brought into contact, they can begin to interact and influence each other's activity. Over time, these interactions can become embedded, forming increasingly interconnected regulatory networks. 

"Regulatory entanglement" balances innovation and stability in genome evolution 

This process, described by the researchers as "regulatory entanglement", may allow genomes to generate new patterns of gene expression while maintaining essential functions. 

Not all aspects of genome structure appear to respond to genome reorganisation in the same way. The researchers found that large structural units of the genome, known as chromatin domains, remained largely stable over evolutionary time.

In contrast, finer-scale connections known as chromatin loops were far more dynamic. These loops bring distant regions of DNA into contact. They varied widely across species, tissues and developmental stages, and were often found near genes involved in key cephalopod traits, including those linked to the nervous system. This suggests that these more flexible regions may be particularly affected by large-scale changes in DNA organisation.

3D structure of DNA shapes evolutionary processes actively 

Together, these findings challenge the idea that genome architecture is a passive consequence of evolution. Instead, they suggest that the 3D organisation of DNA actively shapes how evolution unfolds. In cephalopods, this may have played a key role in the emergence of their unusually complex nervous systems.

Summary

  • Scientists at the University of Vienna reconstructed the 3D organisation of the genome in octopus, squid and cuttlefish to investigate how genome architecture evolved following an ancient burst of genome reorganisation.
  • The study found that this large-scale reorganisation brought previously distant regions of DNA into contact, creating new networks of regulatory interactions that became embedded over evolutionary time.
  • The researchers describe this process as "regulatory entanglement", whereby new DNA interactions become increasingly interconnected, allowing genomes to generate novel patterns of gene regulation while maintaining essential biological functions.
  • The researchers found that not all aspects of the 3D genome respond to genome reorganisation in the same way. Large chromatin domains remained remarkably stable, whereas finer-scale chromatin loops were far more dynamic.
  • The findings challenge the view of genome architecture as a passive consequence of evolution and instead suggest that the 3D organisation of DNA can actively influence evolutionary change.

About the University of Vienna: 

For over 650 years the University of Vienna has stood for education, research and innovation. Today, it is ranked among the top 100 and thus the top four per cent of all universities worldwide and is globally connected. With degree programmes covering 188 disciplines, and approximately 11,000 employees, we are one of the largest academic institutions in Europe. Here, people from a broad spectrum of disciplines come together to carry out research at the highest level and develop solutions for current and future challenges. Its students and graduates develop reflected and sustainable solutions to complex challenges using innovative spirit and curiosity.