The 2025 Nobel prize in chemistry has gone to , and for the development of materials full of cavities that can store and release gases such as carbon dioxide, known as metal-organic frameworks.

“A small amount of such material can be almost like Hermione’s handbag in Harry Potter,” said Heiner Linke, chair of the Nobel Committee for Chemistry. “It can store huge amounts of gas in a tiny volume.”

Tens of thousands of different metal-organic frameworks have now been created. They have many potential applications, from helping to capture CO₂ in chimneys to cleaning up forever chemicals and harvesting water from the air.

In the late 1980s, Richard Robson at the University of Melbourne in Australia was inspired by the ordered structure of diamonds to create the first metal-organic frameworks. Robson realised that it might be possible to use metal ions as nodes, and link them together with carbon-based, or organic, molecules.

When the metal ions and organic molecules are mixed together, they self-assemble into ordered frameworks. While the cavities in the diamond framework are small, the cavities in metal-organic frameworks can be much bigger.

The cavities in the metal-organic frameworks created by Robson were filled with water. It was Susumu Kitagawa at Kyoto University in Japan who first created a framework that was stable enough to be dried out and who managed to fill the empty cavities with gas.

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“He showed that the gases could be taken up, absorbed by the material, and could also be released from the material,” said Olof Ramström, a member of the Nobel Committee for Chemistry.

Kitagawa also went on to create metal-organic frameworks that change shape when gases are added or removed.

Omar Yaghi at the University of California, Berkeley, managed to create frameworks that were even more stable by using metal ion clusters containing zinc and oxygen, and linkers containing carboxylate groups.

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“This is an astonishing framework because it was highly stable. It was stable all the way up to 300 degrees Celsius,” said Ramström. “But even more remarkable was that it contains an enormous surface area. So just a few grams of this porous material, roughly the same as a small sugar cube, contains as much surface area as a large football pitch that is several thousands of square meters.”

Yaghi also went on to show that the cavities in these materials can be made larger, simply by making the linkers longer.

After these fundamental breakthroughs, the field evolved very rapidly, Ramström said. “We see new metal-organic frameworks developed almost every day.”

The 2025 Nobel prize in physiology or medicine has been awarded to three researchers – , and – who discovered a key kind of immune cell that helps stop the immune system attacking itself.

“It unleashed a whole new field in immunology,” said at the Karolinska Institute in Sweden.

Immune cells called T-cells play a key role in immunity by grabbing hold of invasive viruses and bacteria via receptors on their surface. New kinds of T-cells are generated throughout our lives.

Sometimes the receptors on newly-generated T-cells grab hold of our own proteins instead of viral or bacterial ones, which can cause conditions such as type 1 diabetes and rheumatoid arthritis.

The body does have a system for weeding out self-reactive T-cells. T-cells originate in the bone marrow and then migrate to the thymus, a small organ in the chest, where they undergo a selection process. This was long believed to be the only way that self-targeting T-cells are eliminated.

But in 1995, Sakaguchi, now at Osaka University in Japan, showed in mouse experiments that some other cells circulating in the bloodstream must also somehow protect against auto-reactive T-cells. If the thymus of mice is removed after birth, Sakaguchi found, the animals develop autoimmune conditions. But if T-cells from healthy mice are injected into them, this is prevented. His team found that the specific T-cells responsible for this have a protein called CD25 on their surface, and called them CD25 regulatory T-cells.

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Meanwhile, Brunkow, now at the Institute for Systems Biology in Seattle, Washington, and Ramsdell, a scientific adviser at Sonoma Biotherapeutics in San Francisco, California, were studying a strain of mice that is especially likely to get autoimmune conditions. In 2001, Brunkow and Ramsdell found that these mice have a mutation in a gene on the X chromosome called FOXP3.

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People with mutations in this gene are also especially likely to get autoimmune disease, due to a condition known as IPEX syndrome. In 2003, Sakaguchi showed that these two discoveries are linked – the FOXP3 gene plays a key role in the development of the CD25 regulatory cells that his team discovered. Many researchers had been sceptical about Sakaguchi’s earlier claims, said Wahren-Herlenius. But the work of Brunkow and Ramsdell clinched the case.

The discovery of regulatory T-cells could lead to better treatments for a wide range of conditions. On the one hand, boosting the number of regulatory T-cells could help suppress the autoimmune reactions that cause conditions such as type 1 diabetes. On the other, reducing the number of regulatory T-cells could boost the immune response against cancers. A number of clinical trials are now underway.

“Their discoveries have been decisive for our understanding of how the immune system functions and why we do not all develop serious autoimmune diseases,” , chair of the Nobel committee, said in a .

The 2024 Nobel prize in chemistry has been awarded to , �����Ի��� for their work on understanding the structure of proteins, which play vital roles in all living organisms. Hassabis and Jumper, of Google DeepMind, developed an artificial intelligence that predicts the structure of proteins. Baker, at the University of Washington in Seattle, has been recognised for his work on designing new proteins.

Proteins are the molecules that make life happen. All of the key machinery of life is made of proteins, from the muscles that power us and the molecules that read and copy DNA to the antibodies that protect us from infections.

“To understand life, you first need to understand the shape of proteins,” said Heiner Linke, chair of the Nobel committee for chemistry, at a press conference.

All proteins are made of chains of amino acids, and there are around 20 different kinds of these compounds. The shape of proteins is determined by the sequence of amino acids, but the way in which the chains fold up is so complex that predicting a protein’s structure from its sequence is extremely challenging.

“For several decades, this was considered impossible,” said Linke.

Several teams have developed various computational methods of predicting protein structures, but their accuracy was low. Then Hassabis and Jumper developed an AI called AlphaFold.

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The first version of AlphaFold, unveiled in 2018, was an improvement on other methods. The second, released in 2020, was a massive leap forward, predicting two-thirds of protein structures with more than 90 per cent accuracy.

By 2022, AlphaFold had been used to predict the structure of almost all known proteins, with the results made freely available.

“It was an enormous breakthrough,” said Johan Åqvist, a member of the Nobel committee for chemistry. “This is a fantastic resource for chemical and biological research.”

Baker has long been working on the opposite problem, that of designing a protein with a desired structure. The possibilities here are endless – new proteins could be used to do pretty much anything, from treating diseases to creating complex nanomachines.

“David Baker opened up a completely new world of proteins that we had never seen before,” said Åqvist. “It’s a mind-blowing development.”

Baker has created software called Rosetta for doing this, which is also freely available. He and his team first demonstrated that Rosetta worked back in 2003, when they designed a protein, made it and then used a technique called X-ray crystallography to show it had the designed structure.

While Åqvist described this 2003 work as “the big breakthrough”, the protein created was small, simple and didn’t do anything.

Baker himself described the process as more gradual. “It really happened over many years,” he said. “Over the last 20 years, we’ve been able to design proteins with more and more complex and powerful functions.”

“As we got better and better at that, the scope of applications became more and more exciting,” said Baker. “It’s been this huge opening up of possibilities, because the proteins in nature do so many different things. They mediate all the processes in our bodies and in all living things.”

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Baker also gave credit to his colleagues: “I stood on the shoulders of giants. I have had, throughout my career, absolutely wonderful colleagues to work with.”

The award came as a surprise, despite speculation that he might get it, he said. “It’s turning out to be a unique, special day.”

The chemistry prize is the third Nobel awarded so far this year. On 8 October, the 2024 Nobel prize in physics was awarded to John Hopfield and Geoffrey Hinton for their work on artificial neural networks. On 7 October, the 2024 Nobel prize in physiology or medicine went to Victor Ambros and Gary Ruvkun for their discovery that tiny pieces of RNA called microRNAs play a key role in controlling genes.

Last year’s Nobel prize in chemistry went to three of the developers of quantum dots – particles so small that their electrical and optical properties are influenced by quantum physics.

The 2024 Nobel prize in physiology or medicine has been awarded to and for the discovery of tiny pieces of RNA, called microRNAs, that play a key role in regulating gene activity in animals and plants.

The reason they are important is that a single microRNA can control many different genes. A single gene can also be regulated by multiple microRNAs.

“The seminal discovery of microRNAs has introduced a new and unexpected mechanism of gene regulation,” said , the vice-chair of the Nobel committee for physiology and medicine. “These are important for our understanding of embryological development, normal physiology and diseases such as cancer.”

Ambros and Ruvkun made the discovery while studying mutant strains of a nematode worm called �䲹��Դǰ��󲹲��徱�پ���������𲵲��Բ�. Their work began in the 1980s while at the same lab. Ambros then moved to Harvard University and Ruvkun to Massachusetts General Hospital, where they continued studying the mutant strains.

The instructions for making proteins are stored in the DNA in the nucleus of cells. RNA copies of these instructions, called messenger RNAs, carry this information to the protein-making factories outside the nucleus. Messenger RNAs, or mRNAs, can be many thousands of RNA letters long.

One way to control gene activity is to stop mRNAs being made in the first place. Another is to stop mRNAs reaching the protein-making factories. In both cases, the result is to prevent the production of the protein encoded by the gene – or, as biologists say, to switch off the gene.

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MicroRNAs work in the second way. They are tiny pieces of RNA, around 20 base pairs long, whose sequence is complementary to part of one or more mRNAs. When a microRNA binds to its complementary sequence on an mRNA, it typically leads to the breakdown of that mRNA before any protein can be made.

MicroRNAs usually act within a cell, but are sometimes released by cells to control activity elsewhere in a body. In some cases, organisms even release microRNAs to control other organisms. This is usually done by disease-causing organisms, but one symbiotic fungi was recently discovered to release microRNAs to help it colonise tree roots.

Many groups are working on treatments based on microRNAs, . The presence or absence of microRNAs can also help diagnose certain medical conditions.

Ambros and Ruvkun were the first to discover a microRNA, in work done in the 1990s. However, the one they discovered, called lin-4, controls only one gene, and the way it works was assumed to be specific to nematode worms. Because of this, their discovery received little attention.

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In 2000, Ruvkun reported the discovery of another microRNA, called let-7. This controls five genes, and turned out to be widespread in animals. That led to huge interest in microRNAs, and many thousands have now been discovered in a wide array of organisms.

, the secretary-general of the Nobel assembly, said he hadn’t yet contacted Ambros, but had spoken to Ruvkun and his wife. “They were thrilled about the prize and coming to Stockholm,” said Perlmann.

The 2023 Nobel prize in physiology or medicine was awarded to and for working out how to tweak mRNA to avoid its destruction by the immune system, which was key to the development of mRNA vaccines, including the covid-19 ones.

Two scientists whose work led to the mRNA vaccines against covid-19 have been awarded the 2023 Nobel prize in physiology or medicine.

and were awarded the prize for their work on chemically changing strands of mRNA, which made it possible to use them in vaccines.

The technology was licensed by US biotech firm Moderna as well as German biotech firm BioNTech – where Karikó went to work – which then collaborated with the multinational Pfizer. This led to two of the main covid-19 vaccines used in high-income countries, from Moderna and Pfizer/BioNTech.

mRNA is a “messenger” molecule that allows genetic information stored in DNA, in the cell nucleus, to be transported to protein-making factories called ribosomes elsewhere in the cell.

There had long been interest in using mRNA medically to instruct human cells to manufacture proteins that they would not normally make. But if artificially synthesised mRNA is injected into the body, it looks similar to mRNA produced by bacteria – and so is destroyed by various immune chemicals.

While at the University of Pennsylvania in the 1990s, Karikó and Weissman worked out a way to chemically tweak synthesised mRNA so that it looks like the version naturally made by mammalian cells – and so avoid the immune attack.

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In the covid-19 vaccine, the mRNA contains instructions for making the coronavirus spike protein, a molecule on the outside of virus particles. When someone is given the vaccine, their cells start to make this protein, which triggers a normal immune response.

The Moderna and Pfizer/BioNTech vaccines were widely rolled out in high-income countries from early 2021 onwards. Initially they were highly successful at stopping people from being infected with covid-19.

They are less successful at preventing infections with the omicron variants of the virus, which began spreading in late 2021. However, the vaccines are still effective at reducing illness severity and preventing deaths.

Many countries in the northern hemisphere have recently restarted covid-19 booster campaigns before an expected winter surge of the virus – although it is debated whether they should now be offered to most people or only those who are more vulnerable.

The mRNA covid-19 vaccines helped prevent countless deaths and severe ill health from the coronavirus and enabled societies to open up again, said , the secretary of the Nobel Committee for Physiology or Medicine, at an announcement on 2 October. “The work had a major impact on society during the recent pandemic.”

Another advantage of mRNA technology is that it allows vaccines to be made more quickly against any new viruses – such as a bird flu pandemic, said Perlmann. “Future vaccines based on mRNA have the potential to become scalable, fast and flexible.”

They are also being investigated as potential treatments for cancer.