On October 3rd, the 2018 Nobel Prize in Chemistry was awarded to the field of biochemistry, in which Frances H. Arnold of US won half in recognition of her directed evolution of enzymes, and George P. Smith of US and Gregory P. Winter of UK shared the other half in recognition of their phage display technology for peptides and antibodies.
The main contribution of this year’s Nobel Laureate in Chemistry includes evolutionary control, and the use of the same principles of evolutionary change and choice to develop proteins designed to solve human chemistry problems.
In addition to this year’s awards, the Nobel Prize in Chemistry has been awarded 110 times for 181 winners since 1901. However, since Frederick Sanger was awarded twice in 1958 and 1980, respectively, in fact only 180 people won the award.
The Nobel Prize in Chemistry is awarded to six chemical fields: organic chemistry, inorganic chemistry, biochemistry, analytical chemistry, physical chemistry, and theoretical chemistry. The founder of the Nobel Prize, Swede Alfred Nobel, was a chemist who had invented nitroglycerin. According to his will, the Nobel Prize in Chemistry is designed to give people with important discoveries and major achievements in chemistry.
In terms of statistics, the top 5 countries that won the Nobel Prize in Chemistry were the United States, Germany, the United Kingdom, France, and Japan. Among them, the United States led 74 Nobel Prize winners in Chemistry.
Frances Arnold was born in Pittsburgh, USA in 1956 and is currently a professor at the California Institute of Technology. For the first time, she conducted the directed evolution of enzymes, which are proteins that catalyze chemical reactions. Enzymes produced by directed evolution are used to make all products from biofuels to pharmaceuticals.
Directed evolution can also make products more environmentally friendly, including the manufacture of pharmaceuticals, biofuels and even jeans. These environmentally friendly enzymes are often replacements for toxic chemicals.
Since 2017, Arnold and her colleagues have been using directed evolution to make bacteria produce silicon-carbon bonds. Prior to this, only chemists have made silicon-carbon bonds. Studies have shown that bacteria can quickly adapt to new environments and produce new chemical types. More importantly, the discovery can produce products with silicon-carbon bonds in a more environmentally friendly way from lubricants to pharmaceuticals.
Arnold said in an interview, “Evolution is the most powerful engineering method in the world, and we should use it to find new biological solutions to solve problems.”
George P. Smith
George P. Smith was born in Norwalk, United States in 1941. In 1970, he received his Ph.D. from Harvard University. He developed a method called phage display, in which bacteriophage (a virus that infects bacteria) can be used to evolve new proteins.
Phage display is a laboratory technique for studying interactions between protein-protein, protein-peptide and protein-DNA, using phage to associate proteins with the genetic information that encodes them. In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene such that the phage “displays” the protein on its exterior while containing a protein gene in its interior, resulting in a link between the genotype and the phenotype. These display phage can then be screened against other protein, peptide or DNA sequences to detect interactions between the displayed proteins and those other molecules. In this way, large protein libraries can be screened and amplified in a process called in vitro selection, similar to natural selection.
Gregory Paul Winter
Gregory Paul Winter, a British biochemist, was born in Leicester in 1951 and is currently the director of the MRC Institute of Molecular Biology. He graduated from Trinity College of Cambridge University in 1973. He received his Ph.D. from Cambridge University in 1976 and received honors such as MRC Millennium Medal, Royal Medal, and Knight.
Winter’s research mainly focuses on genetics and protein engineering. In his early research, Greg had an interesting idea that all antibodies had the same basic structure, and only a small change in the structure made them specific to the target. He pioneered the technology of humanized antibodies to provide therapeutic antibodies for diseases such as cancer, rheumatoid arthritis and multiple sclerosis.
Winter uses phage display to carry out antibody evolution with the goal of producing new antibody drugs. Adalimumab, the first antibody obtained based on this method, was approved in 2002 for rheumatoid arthritis, psoriasis and inflammatory bowel disease. Since then, antibodies produced using phage display have been used to neutralize toxins to treat autoimmune diseases and metastatic cancers.