biomedical research – Lightsources.org

UK and France launch biomedical and AI health alliance to accelerate research into major diseases

2026/05/292026/06/04

A new partnership will unite expertise, infrastructure and data across borders to accelerate diagnosis, treatment and ultimately prevention of major diseases – starting with women’s health, infectious diseases and pandemic preparedness.

Diamond Light Source, the University of Oxford, Université Paris Cité, the Institut Pasteur and Synchrotron SOLEIL have signed a landmark agreement establishing a major new UK-France scientific alliance designed to strengthen how diseases are understood, diagnosed, treated and ultimately prevented.

The partnership comes at a time when advances in science and technology are generating unprecedented amounts of biological and clinical data, as well as transforming our understanding of human health. But turning that information into faster diagnoses, better treatments and improved disease prevention remains a major challenge across disciplines, institutions and national systems.

The UK–France Strategic Biomedical Alliance in Health and AI has been established to address that challenge by connecting world-leading expertise and national infrastructure into a single collaboration. The interdisciplinary model will unite clinical research, molecular biology, engineering, advanced imaging, data science, artificial intelligence and translational medicine across both countries, making it faster and easier for researchers to connect the technologies, expertise and data needed to tackle complex disease.

Read more on the Diamond website

Image: Dr Jean Susini, Director General, Synchrotron SOLEIL. Sir Thomas Drew KCMG, His Majesty’s Ambassador to France. Professor Richard Cornall, Head of the Nuffield Department of Medicine, University of Oxford. Professor Matthieu Resche-Rigon, Dean of the Health Faculty, Université Paris Cité. Jean-Luc Moullet, Director General for Research and Innovation, French Ministry of Higher Education, Research and Space. Dr Martin Walsh, Interim Director of Life Sciences, Diamond Light Source. Dr Odette Tomescu-Hatto, Director of International Affairs, Institut Pasteur.

Credit: The Department for Science, Innovation and Technology (DSIT)

X-raying auditory ossicles – a new technique reveals structures in record time

2026/01/122026/01/22

Scientists at the Paul Scherrer Institute PSI have refined an X-ray diffraction technique for detecting biological structures from nanometres to millimetres – reducing the time needed to make the measurement from around one day to about an hour. This opens up a wide range of possibilities for biomedical research – from analysing bone and tissue structures to supporting the development of new implants.

Biological materials are masterpieces created by nature. Bones, for example, are extremely hard, yet at the same time elastic enough to withstand lateral forces without breaking easily. This combination of properties results from their hierarchical structure as composite materials – they combine materials that have different structures on different scales. Human-made composite materials are similar in the way they are made up. In reinforced concrete, for example, the concrete component, consisting of cement and sand, can withstand high pressure, while a steel mesh provides high tensile strength and transverse stability.

Until now, examining such biological materials in detail has required the use of several different instruments, such as electron microscopes or classic light microscopes. However, scientists at the PSI Center for Photon Science have now refined an X-ray diffraction technique that was developed at the institute ten years ago, allowing it to be used to characterise materials on scales from nanometres to millimetres simultaneously and much faster than before. A complete scan now only takes about an hour, instead of a whole day.

To demonstrate the efficiency of their method, the researchers used the Swiss Light Source SLS to reveal the alignment of collagen fibres in a human ossicle known as the incus, or anvil. Collagen fibres are thread-like protein structures that provide tensile strength and elasticity to bones. “In doing so, we have taken the leap from a scientific method to a practical technique,” says Christian Appel, postdoctoral researcher and first author of the study. The results have now been published in the journal Small Methods as its cover story. In future, this method could be valuable in areas such as the study of complex tissue, the analysis of bone diseases and the optimisation of implant designs.

Read more on the PSI website

Image: Scientists at PSI were able to observe the local collagen structures in an ossicle by scanning it with an X-ray beam. The different colours of the cylinders indicate how strongly the collagen bundles are spatially aligned in a section measuring 20 by 20 by 20 micrometres.

Credit: © Paul Scherrer Institute PSI/Christian Appel

New antibody-like molecule to prevent infection from malaria

2024/10/112024/11/11

The protein mapping workhorses of the Australian Synchrotron, Macromolecular and Microfocus crystallography beamlines, MX1 and 2, continue to support important biomedical research in the development of vaccines and new therapeutics.

The latest publication from University of La Trobe malaria researchers highlights favourable results with a molecule that could inhibit the ability of malaria parasites to infect cells at different stages of the disease.

The research team led by Professor Michael Foley, Professor Robin Anders and PhD candidate Dimuthu Angage of the La Trobe Institute for Molecular Science showed that the molecule can protect against several different malaria parasite species and was reported in Nature Communications.

In this research featured on the La Trobe University website, they reported that the molecule )WD34 bound with a protein known as AMA1, which is common to many malaria parasite species and is one of two proteins that play a critical role in infection.

“We urgently need broader therapeutic options to combat drug resistance and treatment failures, and this discovery provides some hope for the development of a treatment for all malaria parasite species,” said lead author Professor Michael Foley of La Trobe University in a report on the university website.

AMA1 is a key protein target in malaria vaccines. It helps the malaria parasite invade human and mosquito cells by forming tight junctions with another protein complex. However, AMA1 has many surface variations, which means vaccines based on it only protect against specific strains of malaria.

La Trobe University researchers have identified a new molecule, an i-body, which is similar to a human antibody. This i-body can recognise a common part of AMA1 found in all malaria. The i-body, known as WD34, binds strongly to AMA1 and blocks the parasite from invading red blood cells and liver cells.

The MX2 beamline was used to determine the structure of the WD34-AMA1 complexes.

Read more on ANSTO website