The first pharmaceutical based on this method, adalimumab, was approved in 2002 and is used for rheumatoid arthritis, psoriasis and inflammatory bowel diseases. Since then, phage display has produced antibodies that can neutralise toxins, counteract autoimmune diseases and cure metastatic cancer.
The Royal Swedish Academy of Sciences announced the 2018 Prize this morning with one half to Frances H. Arnold and the other half jointly to George P. Smith and Sir Gregory P. Winter.
The Nobel Assembly said: “The 2018 Nobel Laureates in Chemistry have taken control of evolution and used it for purposes that bring the greatest benefit to humankind. Enzymes produced through directed evolution are used to manufacture everything from biofuels to pharmaceuticals. Antibodies evolved using a method called phage display can combat autoimmune diseases and in some cases cure metastatic cancer.”
Winter, the Master of Trinity College, is a genetic engineer and is best known for his research and inventions relating to humanised and human therapeutic antibodies. Sir Gregory is a graduate of Trinity College and was a Senior Research Fellow before becoming Master.
His research career has been based almost entirely in Cambridge at the Medical Research Council’s Laboratory of Molecular Biology and the Centre for Protein Engineering, and during this time he also founded three Cambridge biotech companies based on his inventions: Cambridge Antibody Technology (acquired by AstraZeneca), Domantis (acquired by GlaxoSmithKline) and Bicycle Therapeutics.
Winter becomes the 107th Affiliate of Cambridge to be awarded a Nobel Prize. Born in 1951 in Leicester, Sir Greg studied Natural Sciences at Trinity College, Cambridge, and was awarded his PhD, also from Cambridge, in 1977.
"It came as a bit of a shock, and I felt a bit numb for a while. It's almost like you're in a different universe," said Winter, on hearing he had been jointly awarded the Prize.
"For a scientist, a Nobel Prize is the highest accolade you can get, and I'm so lucky because there are so many brilliant scientists and not enough Nobel Prizes to go around."
The University's Vice-Chancellor, Professor Stephen Toope, said: "I am thrilled to hear that Sir Greg Winter has been awarded this year’s Nobel Prize in Chemistry. Greg’s work has been vital in the development of new therapies for debilitating health conditions such as rheumatoid arthritis, and has led to breakthroughs in cancer care. These advances continue to transform the lives of people across the world.
"It gives me the greatest pleasure, on behalf of our community, to congratulate the University of Cambridge’s latest Nobel Prize winner.”
Patrick Maxwell, Regius Professor of Physic and Head of the School of Clinical Medicine at the University of Cambridge, said: “I am absolutely delighted that Sir Greg’s work has been recognised with a Nobel Prize. The work for which the prize is awarded was carried out on the Cambridge Biomedical Campus. It directly led to the power of monoclonal antibodies being harnessed for treatment of disease. His inventions really have produced silver bullets that have transformed the way medicine is practised.”
Professor Sir Alan Fersht, former Master of Gonville and Caius, collaborated with Winter on early protein engineering work. "Greg Winter is an outstandingly creative scientist of a practical bent," he said.
"He has applied his skills and imagination to the benefit of humankind to create, amongst other inventions, novel engineered antibodies that have formed the basis of a new pharmaceutical industry to treat disease and cancer. It is a thoroughly worthy Nobel Prize," Fersht said.
Professor Dame Carol Robinson, Royal Society of Chemistry president, said: “Today’s Nobel Prize in chemistry highlights the tremendous role of chemistry in contributing to many areas of our lives including pharmaceuticals, detergents, green catalysis and biofuels. It is a great advert for chemistry to have impact in so many areas.
“Directed evolution of enzymes and antibody technology are subjects that I have followed with keen interest; both are now transforming medicine. It would have been hard to predict the outcome of this research at the start – this speaks to the need for basic research.
“I am delighted to see these areas of chemistry recognised and congratulate all three Nobel Laureates.”
Frances H. Arnold, who also shared today's Prize, conducted the first directed evolution of enzymes, which are proteins that catalyse chemical reactions. Since then, she has refined the methods that are now routinely used to develop new catalysts. The uses of Frances Arnold’s enzymes include more environmentally friendly manufacturing of chemical substances, such as pharmaceuticals, and the production of renewable fuels for a greener transport sector.
In 1985, George Smith developed an elegant method known as phage display, where a bacteriophage – a virus that infects bacteria – can be used to evolve new proteins.
More details on previous Cambridge winners can be found here:
https://www.cam.ac.uk/research/research-at-cambridge/nobel-prize
You can read more about the 2018 Nobel Prize in Chemistry here:
https://www.nobelprize.org/uploads/2018/10/popular-chemistryprize2018.pdf
Sir Gregory Winter, awarded the
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in Chemistry, has used phage display to produce new pharmaceuticals. Today phage display has produced antibodies that can neutralise toxins, counteract autoimmune diseases and cure metastatic cancer.
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— The Nobel Prize (@NobelPrize)
October 3, 2018
