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Merrifield (Merrifield), Bruce R.

( American biochemist and Nobel Prize in Chemistry, 1984)

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Biography Merrifield (Merrifield), Bruce R.
genus. July 15, 1921
American biochemist Robert Bruce Merrifield was born in Fort Worth (Texas). He was the only son in the family Louren (Lucas) Merrifield, and George Merrifield. Two years after his birth the family moved to California Merrifield and during the Great Depression of the 30-ies. continued to move frequently from place to place, tk. Father M. (furniture retailer) is constantly searching for work. M. once estimated that he had visited about 40 schools before his family settled in Montebello (California). Here, learning in high school, the future scientist interested in chemistry. Here he engaged in a school astronomy club, constructed a small telescope.
After graduating in 1938. high school, M. enrolled in Junior College in Pasadena, but the following year moved to the University of California at Los Angeles, where he began to study chemistry. Simultaneously, he worked in a laboratory Max Dunn, where at this time synthesized degidroksifenilalanin - amino acid, which is involved in the transmission of nerve impulses and is used to treat Parkinson's disease. Received the University of California in 1943. BA, M. the year worked as a chemist in the Research Foundation, Philip R. Park, and then again returned to university. Scholarship from 'Anheyzer-Bush Incorporation' allowed him to continue his studies: M. graduate studies. Later, working as an assistant researcher in the School of Medicine, University of California at Los Angeles (1948 ... 1949), M. studied yeast purines and pyrimidines, and developed a system of biological qualitative analysis to verify how they contribute to the growth of bacteria. (Purines and pyrimidines represent a cyclic nitrogenous organic bases, which are part of biologically important compounds - such as nucleotides and nucleic acids.) Once in 1949. M. was awarded a doctoral degree in chemistry, he was appointed assistant in biochemistry at the Rockefeller Institute for Medical Research (now Rockefeller University) in New York. This institute scientist remained until the end of his scientific career. He became a research assistant here (1953), then Associate Professor (1958) and, finally, full professor (1966).
In 1953, Mr.. M. engaged in protein chemistry. 'Proteins - are the key components of all living organisms, - he explained later. - All enzymes are catalysts of biological reactions, and many of them regulating hormones - proteins. If we want to understand and learn how to control what happens in the body, we must first know the composition, structure and function of each individual protein '.
. The protein molecule is a chain of amino acids linked by peptide chains
. In an effort to understand the structure of these large and very complex organic molecules, scientists are trying to synthesize them from their chemical components. Two classic ways of binding amino acids are reflected in the step and the fragmentation patterns. According to a stepped method (developed in the early XX century. Emil Fischer), amino acids from one adds to the growing peptide chain. On the fragmentation method, the amino acids initially bound in a short peptide fragments, which are then connected to the formation of large peptides. Either of these two methods at each stage of a coherent synthesis necessary to protect (or hide) all the chemically active groups in the growing peptide molecule to interact with only the necessary parts. Moreover, open or vulnerable groups also have to activate in order to able to be formed peptide bond.
. The sequence of protection, activation, synthesis and removal of protecting groups must be repeated until such time has not yet formed a complete peptide molecule required composition
. By-products of each of the previous reactions and reagents (protectors deprotektory and activators), which were used at each stage, it was necessary to wash, and the resulting peptide - cleaned before adding the next amino acid. Since at each stage inevitably loses a small portion of the desired product, the final peptide represents only a small fraction of potential. Although these classical methods allowed Vincent du Vigneaud synthesize oxytocin and vasopressin, and M. - To prepare peptides of 20 and 40 amino acids in a randomly chosen sequence, these methods were inefficient, time-consuming and labor.
In 1959, Mr.. M. wrote in his research notebook: 'need a quick, quantitative, automated method for the synthesis of long peptide chains'. It came from the fact that if the first amino acid formed insoluble carrier, the unwanted by-products and reagents can be washed out from the reaction vessel after each stage, and the growing peptide is thus unaffected. If so, the final yield would increase significantly. And when the synthesis process is completed, the final peptide can be separated from its carrier and purified by conventional methods. Supported Dilworthy Woolley of the Rockefeller Institute M. spent the next three years developing a better method of peptide synthesis.
The most effective medium for the first amino acid proved to be a polymer of styrene and divinylbenzene. In 1962. M. reported that in a relatively short period of time, a new method, called solid phase peptide synthesis, has provided a great way of artificial peptides - almost 100 percent of the predicted number of. Applying this method, M. and his colleagues synthesized nonapeptidny (consisting of 9 amino acids) hormone bradykinin - potent agent that causes vasodilatation.
. Their next task was to design an apparatus capable of automated peptide synthesis
. Working with assistant John Stewart in the basement of his house and with the assistance of Nils Dzhernberga of the workshop on manufacturing equipment at the Rockefeller Institute, M. in 1965. created the first working model of automated devices for solid-phase peptide synthesis. This device is a container for amino acids and reagents - the reaction vessel with automatic inlet and outlet valves and policy mechanisms that regulate the sequence of the process.
. With the apparatus constructed M
. and his colleagues synthesized several peptide hormones, including bradykinin, oxytocin, and angiotensin (octapeptide, which regulates blood pressure). They also received the protein insulin (containing 51 amino acids in two chains) in only 20 days, whereas previously this process takes several months. Opponents of the new technology have complained that obtained with the help of its peptide products were not pure. Recognizing that the problem of purity existed from the beginning of their work on the study of peptide synthesis, M. opted for a pragmatic approach to 'best use of currently available methods of synthesis, isolation and characteristics of the reaction products'. 'Improvements in the methods of separation appear continuously, - he said. - And what now seems unattainable, tomorrow may be surprisingly simple '. The problem of purification of the reaction product will soon helped to develop a method to solve high-performance liquid chromatography.
In 1969. with Bernd Gouttes M. completed the first successful synthesis of the naturally occurring enzyme ribonuclease. Ribonuclease, alternating sequence of amino acids which was established Stanford Moore and William X. Stein in 1960, was the subject of research in the Rockefeller Institute for over 30 years. Method M. provides for 369 chemical reactions and 11 931 single stage, which required several weeks of continuous operation of solid-phase synthesizer.
Developed M. technology of solid-phase synthesis, . which neither he, . nor Rockefeller University never patented, . widely used in other institutions and commercial laboratories for peptide hormones, . neuropeptides, . toxins, . protein growth factors, . antibiotics, . nucleotides and nucleic acids,
. Most often, this technology is used in the synthesis of peptides containing up to 50 amino acids. Wife M. (nee Elizabeth Furlong), working in the laboratory, scientists at Rockefeller University, uses an automated solid-phase technology, exploring the possibility of protein synthesis of interferon. Interferon, which contains 166 amino acids, can serve as a valuable therapeutic agent for treatment of viral diseases and tumors.
In 1985, Mr.. M. was awarded the Nobel Prize in Chemistry for his proposed methodology for chemical synthesis on solid matrices. 'It is a new approach [M.] to organic synthesis has created new opportunities in the field of peptide-protein chemistry and nucleic acids - Bendt Lindberg said in his opening speech on behalf of the Royal Swedish Academy of Sciences. - He is greatly stimulated the development of biochemistry, molecular biology, medicine and pharmacology, as well as of great practical importance for the development of new drugs and ekarstvennyh for Genetic Engineering '.
. We Merrifield spouses who marry in 1948, six children
. They live in Kresskille (New Jersey).
Part of his free time, scientists have paid Boy Scout movement. In 1968. M. was a visiting professor at the Nobel Uppsala University in Sweden. Since 1969. He worked as deputy editor of the International Journal for the Study of peptides and proteins ( 'International Journal of Peptide and Protein Research'). Among the many awards, . which awarded scholar, . include: the Albert Lasker Award for basic medical research (1969), . International Award Gardner Fund (1970), . award for creative work in the synthesis of organic compounds (1972) and the Nichols Medal (1973) American Chemical Society,
. M. - Member of the U.S. National Academy of Sciences. He was awarded honorary degrees from the University of Colorado, as well as Yale and Uppsala University.

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Merrifield (Merrifield), Bruce R., photo, biography
Merrifield (Merrifield), Bruce R., photo, biography Merrifield (Merrifield), Bruce R.  American biochemist and Nobel Prize in Chemistry, 1984, photo, biography
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