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Robert Bruce MerrifieldNobel Prize in Chemistry 1984.
Date of Birth: 15.07.1921
Country:  USA |
Content:
Biography of Robert Bruce Merrifield
Robert Bruce Merrifield was an American biochemist and the recipient of the 1984 Nobel Prize in Chemistry. He was born in the family of George and Laurence Lucas Merrifield as their only son. Two years after his birth, the Merrifield family moved to California and during the Great Depression of the 1930s, they continued to move from place to place as his father, a furniture salesman, constantly searched for work. Merrifield attended about 40 schools before his family settled in Montebello, California. It was here, while attending high school, that he became interested in chemistry and constructed a small telescope. After graduating from high school in 1938, he entered Junior College in Pasadena, but transferred to the University of California, Los Angeles the following year, where he began studying chemistry. At the same time, he worked in M. Dunn's laboratory, where they were synthesizing dehydroxyphenylalanine, an amino acid used for the treatment of Parkinson's disease. Merrifield received his bachelor's degree from the University of California in 1943 and then worked as a chemist at the F.R. Park Research Foundation for a year before returning to the university and entering graduate school. Later (1948-1949), while working as a research assistant at the School of Medicine at the University of California, Los Angeles under D.W. Woolley, who had a profound influence on his development, Merrifield studied yeast purines and pyrimidines and developed a system for the qualitative bioanalysis of how they promote bacterial growth.
In 1949, he obtained his doctoral degree in chemistry and was appointed as a biochemistry assistant at the Rockefeller Institute for Medical Research (now Rockefeller University) in New York. He remained at this institute for his entire scientific career, serving as a research associate (1953), adjunct professor (1958), and finally, full professor (1966). Here, he developed an automated system for peptide synthesis and in 1985, was awarded the Nobel Prize "for the development of methodology for chemical synthesis on solid phase."
In 1953, Merrifield began studying protein chemistry. "Proteins are the key components of all living organisms," he later explained. "All enzymes that act as catalysts in biological reactions and many hormones that regulate them are proteins. If we want to understand and learn to control what happens in the body, we must first know the composition, structure, and function of each individual protein." In 1959, Merrifield wrote, "There is a need for a fast, quantitative, automated method for the synthesis of long peptide chains." If the first amino acid is formed on an insoluble carrier, then unwanted by-products and reagents can be washed out of the reaction vessel after each stage, while the growing polypeptide remains unaffected. When the synthesis process is complete, the final polypeptide can be separated from the carrier and purified using conventional methods. With Woolley's support, he spent the next three years developing a more advanced method for peptide synthesis.
A copolymer of styrene and divinylbenzene proved to be an effective carrier for the first amino acid. In 1962, Merrifield announced that the new method, called solid-phase peptide synthesis, provided almost quantitative yields of target polypeptides in a relatively short period of time. Using this method, Merrifield and his colleagues synthesized the nonapeptide hormone bradykinin, a potent vasodilator. The next challenge was to construct a device capable of automating peptide synthesis. Working in the basement of his home with the assistance of J. Stewart and a technician from the workshop, Merrifield created the first working model of an automated device for solid-phase peptide synthesis in 1965. This device consisted of a container for amino acids and reagents - a reaction vessel with automatic inlet and outlet valves and a program mechanism that regulated the sequence of the process.
Using the constructed apparatus, Merrifield and his colleagues synthesized several peptide hormones, including bradykinin, oxytocin, and angiotensin (an octapeptide that regulates blood pressure). They also obtained insulin (which contains 51 amino acids in two chains) in just 20 days, whereas previously this process took several months. Critics of the new technology claimed that the peptide sequences obtained using it were not pure. Acknowledging that the purity problem had existed from the beginning of his work, Merrifield preferred a pragmatic approach of "using the best available methods of synthesis, isolation, and characterization of reaction products." He stated, "Improvements in separation methods are constantly emerging, and what seems unattainable today may turn out to be surprisingly simple tomorrow." The problem of purifying the reaction product was soon solved with the development of high-performance liquid chromatography.
In 1969, Merrifield completed the first successful synthesis of the enzyme ribonuclease. Merrifield's method involved 369 chemical reactions and 11,931 individual stages, requiring several weeks of continuous operation of the solid-phase synthesizer.
Merrifield's method revolutionized chemical synthesis and had a profound impact on the development of various fields such as biochemistry, molecular biology, biotechnology, and more. According to many authoritative scientists, Merrifield's discovery had a significant influence on the thinking of specialists.
In 1968, Merrifield was invited as a Nobel Professor to Uppsala University in Sweden. Since 1969, he has been serving as the deputy editor-in-chief of the journal "International Journal of Peptide and Protein Research."
Merrifield currently resides in Cresskill, New Jersey.
Works: Solid-phase peptide synthesis: The synthesis of a tetrapeptide // J. Am. Chem. Soc. 1963. V. 85; Solid-phase synthesis of the cyclododecadepsipeptide valinomicin // J. Am. Chem. Soc. 1969. V. 91 (with B.F. Gisin, D.C. Tosteson).
