That's all folks
And there we have it: the Nobel science prizes are done for another year. Yes, the awards come in for a lot of stick, and much of it is justified. But they do force us to stand back and look at what scientists and engineers have achieved. On Monday, we saw the medicine prize awarded for checkpoint inhibitors, the radical new drugs that help direct the full force of the immune system on to cancer. On Tuesday, the physics prize went to the sci-fi technology of optical tweezers, which allow researchers to hold live bacteria in beams of light. The same prize also celebrated the development of intense, ultrashort laser pulses, now used in corrective eye surgery millions of times a year. And today, of course, the chemistry prize went for the transformational methods of directed evolution and phage display. Along the way, Donna Strickland at the University of Waterloo became the first woman to win the Nobel prize in physics for 55 years; Frances Arnold became only the fifth woman to win the chemistry prize; and Arthur Ashkin, aged 96, became the oldest person to receive any Nobel prize. Congratulations to them all. Thanks to everyone who joined us for the ride. Until next year, bye bye.
I’ll wrap up with some wonderful words from George Smith, reached by the Associated Press shortly after he won the prize. I can’t think of another laureate who has so clearly stressed the importance of the work they built on.
Very few research breakthroughs are novel. Virtually all of them build on what went on before. It’s happenstance. That was certainly the case with my work. Mine was an idea in a line of research that built very naturally on the lines of research that went before.
Smith learned of the prize in a pre-dawn phone call from Stockholm.
It’s a standard joke that someone with a Swedish accent calls and says you won! But there was so much static on the line, I knew it wasn’t any of my friends.
Winter on antibody treatments
Here’s a fascinating video of Sir Gregory Winter speaking in 2016 about the power of therapeutic monoclonal antibodies. On trying a humanised antibody in a cancer patient for the first time at Cambridge, doctors saw a dramatic effect. Winter went in to see here and confessed that he hadn’t known if the treatment would help her. She said: “It only has to buy me a couple of months...my husband is dying and I want to be with him when he dies.”
"It was considered the lunatic fringe"
“When I started engineering proteins, I didn’t know how hard it would be,” said Frances Arnold in 2014 on being inducted to the National Inventors Hall of Fame. “And after a number of experiments that were failures, I realised that I would have to find a different approach to solving the problem.”
“When I started publishing papers demonstrating that I could make more stable enzymes, that I could alter their substrate specificity, that I could make them much more active, these were things that no one knew how to do,” she said.
“Twenty five years ago, it was considered the lunatic fringe. Scientists didn’t do that. Gentlemen didn’t do that. But since I’m an engineer and not a gentleman, I had no problem with that.”
Some graphics might help. Here are some, courtesy of the Nobel assembly. First up, how Frances Arnold’s directed evolution works:
And here is a run-through of George Smith’s phage display process:
And finally, here’s how Sir Gregory Winter used phage display to produce therapeutic antibodies:
So what did the winners do?
In 1993, Frances Arnold performed the first directed evolution of enzymes. She has since refined the methods that are now used around the world to develop new catalysts. Among their applications are more environmentally friendly chemical manufacturing to produce substances such as pharmaceuticals and renewable fuels for greener transport systems.
In 1985, George Smith developed a process that is now known as phage display. It uses a bacteriophage – a virus that infects bacteria – to evolve new proteins. Winter took up the technology and used it for the directed evolution of antibodies, with the aim of making new drugs. The first one based on phage display, adalimumab, was approved in 2002 and is used for rheumatoid arthritis, psoriasis and inflammatory bowel diseases. Phage display has since been used to make antibodies that can neutralise toxins, counteract autoimmune diseases and cure metastatic cancer.
Frances Arnold, who becomes the fifth woman to win the Nobel prize in chemistry, has been on the line to the Royal Swedish Academy of Sciences in Stockholm. But the line was so bad no one could hear what she was saying. What a shame.
Frances Arnold performed the first “directed evolution” of enzymes, which are proteins that catalyse chemical reactions. Enzymes produced through directed evolution are used to manufacture everything from biofuels to pharmaceuticals.
George Smith developed a method called phage display, where a bacteriophage – a virus that infects bacteria – can be used to evolve new proteins.
Sir Gregory Winter used phage display to produce new pharmaceuticals. Today phage display has produced antibodies that can neutralise toxins, counteract autoimmune diseases and cure metastatic cancer.
The announcement from the Royal Swedish Academy of Sciences states that it has decided to award the Nobel Prize in Chemistry 2018 with one half to
Frances H Arnold, at California Institute of Technology, Pasadena, USA
“for the directed evolution of enzymes”
and the other half jointly to George P Smith at the University of Missouri, Columbia, USA, and Sir Gregory P Winter at the MRC Laboratory of Molecular Biology in Cambridge, UK
“for the phage display of peptides and antibodies”.
One of the winners, Sir Gregory Winter, is at the MRC’s Laboratory of Molecular Biology in Cambridge. This is now its 12th Nobel prize.
A committee member is explaining how this year’s prize “awards a revolution based on evolution”, and goes to scientists who “applied the principles of Darwin in the test tube”.
And the winners of the 2018 Nobel prize in chemistry are:
Here we go. The committee has arrived.
We’re only a few minutes off now. Let’s hope the announcement gets a good reaction. (Sorry.)
How does the Nobel committee decide who wins the prize? The Royal Society of Chemistry’s magazine, Chemistry World, sat down with Bengt Nordén, the former chair of the chemistry prize selection committee, and asked him to spill the beans.
Here’s the room where the announcement will be made. Can anyone spot a portrait of a woman on those walls?
Runners and riders
There are people out there who seem almost destined to get the call from Stockholm one year or another. It’s about time the phone rang for John B Goodenough at the University of Texas in Austin. He invented lithium-ion batteries, without which we’d struggle to have laptops, mobile phones, cameras and tablets. If he wins, the 96-year-old will become the joint oldest laureate in history. His co-nonagenarian? That would be Arthur Ashkin, who shared the physics prize on Tuesday.
Or will the prize go to the pioneers of gene editing? To my mind it hasn’t delivered the clinical benefits to warrant the medicine prize, but the chemistry prize is a real possibility. I can see it going to Emmanuelle Charpentier, Jennifer Doudna and Feng Zhang for developing Crispr, or “clustered regularly interspaced short palindromic repeats” if you wish. It’s the most popular genome editing tool around. The enormous potential of the technology to correct fault genes has fuelled a fierce patent battle between Doudna’s University of California in Berkeley and Zhang’s Broad Institute of MIT and Harvard. Awarding the prize for Crispr would certainly boost the diversity of the chemistry laureates. Only four women have ever won the prize: Ada Yonath in 2009, Dorothy Crowfoot Hodgkin in 1964, Irène Joliot-Curie in 1935 and Joliot-Curie’s mum, Marie Curie, in 1911.
On the hardcore chemistry side a good candidate is Omar Yaghi, another Berkeley scientist, who won the Wolf prize earlier this year. He invented new materials called MOFs (metal-organic frameworks) and COFs (covalent organic frameworks) that have extremely high surface areas and have found uses in hydrogen storage and separation; clean water production and super-capacitors.
If I had to choose, I’d plump for Goodenough.
The 2017 winners
Last year, the chemistry honours went to Jacques Dubochet, Joachim Frank and Richard Henderson, who found a way to produce images of the molecules of life frozen in time. Known as cryo-electron microscopy, it allowed biomolecules to be visualised in their natural state for the first time, triggering a “revolution in biochemistry”, the Nobel committee said at the time. Like ginormous spinning molecules? Then you’ll love cryo-electron microscopy. Here’s some now.
A Nobel finale
And so to the third and final Nobel science prize of 2018. Today we shall hear who has won the chemistry prize, an award that comes with buckets of kudos and 9m Swedish kronor – that’s £770,000 unless the pound has fallen again.
On Monday, James Allison at the University of Texas’s MD Anderson Cancer Center and Tasuku Honjo at the University of Kyoto shared the Nobel prize in medicine for checkpoint inhibitors – drugs that harness the body’s immune system to combat cancer. It was the first time a Nobel prize had been awarded for a cancer therapy.
Yesterday, American physicist Arthur Ashkin, Gérard Mourou from France, and Donna Strickland in Canada shared the Nobel prize in physics. Ashkin, who bagged half of the prize, invented “optical tweezers” – a tractor beam-like technology that allows scientists to grab and manipulate atoms, viruses and bacteria. At 96, he is the oldest ever recipient of any Nobel prize.
Mourou and Strickland shared the remaining half of the prize for developing ultrafast laser pulses that are now used in laser machining and in millions of corrective eye surgeries a year. Strickland is the first woman to win the physics prize in 55 years and only the third in history, after Maria Goeppert Mayer in 1963 and Marie Curie in 1903.
Who will receive the call from Stockholm today? We’ll find out at 10.45am UK. Or thereabouts.