||Click here to view the the letter from APS President, Jane Aldrich.
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Click here to view the symposium tribute to Bruce Merrifield.
Tribute to Prof. R. Bruce Merrifield - Page 1 of 2
Bruce Merrifield, John D. Rockefeller Jr. Professor Emeritus at The Rockefeller University, died Sunday, May 14, 2006, at his home in Cresskill, NJ, after a long illness. He was 84. Thus, the peptide community lost one of the most innovative scientists of the 20th century.
In the 1960s, Merrifield earned world renown for the development of a rapid, automated procedure for synthesizing peptides and proteins which he named solid phase peptide synthesis. This method makes it possible to do in a matter of days what would previously have taken years to achieve, if at all. Merrifield's discovery has been credited with making possible the systematic exploration of the structural bases of the activities of enzymes, hormones and antibodies. In recent years, the method has been especially important for the rapid discovery of new, active therapeutics.
First reported in 1962, solid phase peptide synthesis uses an insoluble solid support to anchor the carboxyl terminal amino acid of the peptide. Merrifield and his colleagues, John Stewart and Maurice Manning, along with his graduate students Garland Marshall and Arnold Marglin, demonstrated the validity and generality of the technique with syntheses of bradykinin, desamino-oxytocin, angiotensin, and insulin. Concurrently, Merrifield worked with Stewart and Nils Jernberg to design and build a machine to automate the method. In 1969, Merrifield and Bernd Gutte announced that they had used the machine for the first synthesis of an enzyme, ribonuclease A, consisting of 124 amino acids. This work proved not only that medium size proteins can be synthesized by the stepwise solid phase method, but that the primary sequences of proteins determine their tertiary structures and ultimately their biological activities.
Researchers all over the world have been using the procedure to make other important molecules, including somatostatin, beta-endorphin, ACTH, and trypsin inhibitor. The technique is also used to study the effects of synthetic antigenic peptides on the production of specific antibodies, work that has important implications in disease research.
Merrifield dedicated a large part of his research to refining solid phase synthesis in order to tackle ever more difficult challenges. He and his colleagues worked on an important group of peptide antibiotics and on the design and synthesis of good antagonists of the hormone glucagon, which may be useful for the control of blood sugar in diabetics.
The solid phase principle has also been adapted to the synthesis of oligonucleotides as well as carbohydrates and other organic molecules. In recent years, the method has been especially useful for multiple syntheses of peptides, and for combinatorial synthesis of peptide and non-peptide libraries that are important for the rapid discovery of new active drugs.
In 1984, the Royal Swedish Academy of Sciences awarded the Nobel Prize in Chemistry to Merrifield "for his development of methodology for chemical synthesis on a solid matrix."
In 1998, Merrifield was named one of 75 "distinguished contributors to the chemical enterprise" by Chemical & Engineering News, the news magazine of the American Chemical Society, in a special issue marking the magazine's 75th anniversary. In 2003, the Journal of the American Chemical Society listed Merrifield's classic 1963 paper, in which he first described the solid phase synthesis technique, as the fifth most cited paper in the journal's 125-year history. Most recently, in June 2006, this classic paper was recognized by the Division of the History of Chemistry of the American Chemical Society as a Chemical Breakthrough Publication.