Vincent du Vigneaud | Biography

Vincent du Vigneaud, an American biochemist, received the 1955 Nobel Prize for Chemistry for his breakthrough achievement of synthesizing oxytocin--a hormone released by the posterior pituitary gland used to induce labor and lactation in pregnant women, and for his work with sulfur. Throughout his career, du Vigneaud was recognized for isolating and synthesizing penicillin and the hormone vasopressin , which is used to suppress urine flow, identifying the chemical composition of insulin, discovering the structure of vitamin H, otherwise known as biotin, and his pioneering work with methyl groups .

Du Vigneaud was born in Chicago, Illinois, on May 18, 1901, to Alfred, an inventor and designer of machines, and Mary Theresa (O'Leary) du Vigneaud. Early in his high school education in Chicago's public school system, du Vigneaud demonstrated an aptitude for chemistry and physiology. He constructed a laboratory in his parents' basement, where he carried out his first experiments. Du Vigneaud enrolled in the University of Illinois as an organic chemistry major and graduated in 1923. He stayed on to earn a masters degree in 1924, studying under C. S. Marvel. Also in 1924, du Vigneaud married Zella Zon Ford. Both of their children went on to become doctors. Their son, Vincent du Vigneaud, Jr., became an obstetrician and gynecologist, and their daughter, Marilyn Renee Brown, became a pediatric gastroenterologist.

From 1924 to 1925, du Vigneaud was an assistant biochemist at the University of Pennsylvania's Graduate School of Medicine and also worked in Philadelphia General Hospital's clinical chemistry laboratory. He then moved to the University of Rochester in New York to study for his Ph.D. under John R. Murlin at the School of Medicine. For his doctoral research, he undertook an examination of the chemical makeup of insulin, the protein hormone and sulfur compound that is secreted by the islets of Langerhans located in the pancreas. Du Vigneaud's investigations, which were inspired by a lecture given by renowned biochemist W. C. Rose at the University of Illinois, sparked a lifelong interest in the range of sulfur compounds, but especially the sulfur-containing amino acids methionine, homocystine, cystine, cysteine, and cystathionine.

After receiving his doctorate in 1927, du Vigneaud became a National Research Council fellow. He worked first at Johns Hopkins Medical School's Department of Pharmacology under John J. Abel, where he continued his research into the structure of insulin. His suspicion that insulin was a derivative of the amino acid cystine was justified when he succeeded in isolating cystine from insulin crystals. He was thereby able to prove that insulin consists only of amino acids and an ammonia by-product.

Du Vigneaud left the United States for Germany in 1928 on a brief overseas tour. He first stopped at the Kaiser Wilhelm Institute in Dresden, where he worked under Max Bergman, an expert on the chemistry of amino acids and peptides (chains of amino acids). Du Vigneaud later turned down an assistantship position with Bergman to proceed to the University of Edinburgh's Medical School, where he worked with biologist George Barger. He also spent time at the University College Hospital Medical School at the University of London, where he worked with Charles Harrington.

Upon returning to the United States, du Vigneaud joined the University of Illinois's physiological chemistry staff under his mentor, W. C. Rose. In 1932, he left his alma mater to take up a position as head of the Department of Biochemistry at the George Washington University School of Medicine in Washington, DC. One of his innovations there was to add a course in biochemistry to the medical school curriculum. His own research lead him to investigate his hypothesis that insulin's blood sugar-lowering effects were related to disulfide bonds of cystine.

In 1936 he and his staff succeeded in artificially creating glutathione, a tripeptide containing the amino acids cysteine, glycine, and glutamic acid, that is widely occurring in plant and animal tissues and which plays a vital part in biological oxidation-reduction processes and the activation of some enzymes. He also continued to pursue his research into insulin . By the following year, he was in a position to prove that the amino acid cystine comprises insulin's entire complement of sulfur, and that insulin can be deactivated by the reduction of its bonds of insulin by cystine or glutathione. Also in the late 1930s, du Vigneaud's work with methionine revealed how the body shifts a methyl group (CH₃) from one compound to another.

In 1938 du Vigneaud was appointed head of Cornell University Medical College's biochemistry department. Within two years, he had succeeded in isolating biotin (vitamin H). He spent the next few years carefully studying the substance and by 1942, had figured out its structure. He next turned to the human posterior pituitary gland, especially the study of the hormones oxytocin and vasopressin that it produces. Oxytocin is known to stimulate the contraction of uterine muscles and the secretion of milk in women during labor. Vasopressin, also known as the antidiuretic hormone, is a polypeptide hormone responsible for causing increased blood pressure and decreased urine flow. Du Vigneaud and his colleagues managed to isolate a highly purified form of these hormones from the pituitary gland and set about discovering their chemical nature.

To his surprise, du Vigneaud discovered that oxytocin is made up of only eight amino acids. Most proteins are comprised of several hundred amino acids. It took du Vigneaud another ten years to determine their sequence in an oxytocin molecule. Once he had cracked this puzzle, he was finally able to synthesize oxytocin. The importance of du Vigneaud's achievement lay not only in its making available an unlimited supply of the protein, but also in the light it shed on the relationship between molecular structure and biological function. The synthetic protein was tested on pregnant women at the Lying-in Hospital of the New York Hospital-Cornell Medical Center, where it was found to be as effective in inducing labor and milk flow as pure oxytocin. In 1946 the journal Science announced another du Vigneaud breakthrough: his synthesis of penicillin. Although du Vigneaud carried out the decisive experiments at Cornell University, it was one of the greatest international efforts of its kind, said Science, the culmination of five years of concerted effort by thirty-eight teams of scientists in the U.S. and Britain.

Du Vigneaud's illustrious scientific career was widely recognized. In 1955, he was awarded the Nobel Prize for Chemistry for "his work on biochemically important sulfur compounds and especially for the first synthesis of a polypeptide hormone." Du Vigneaud's other awards include the Nichols Medal of the American Chemical Society in 1945, the Association of Medical Colleges' Borden Award in the Medical Sciences in 1947, the Public Health Association's Lasker Award in 1948, the Osborne and Mendal Award of the American Institute of Nutrition in 1953, Columbia University's Charles Frederick Chandler Medal, and the Willard Gibbs Medal of the American Chemical Society. In addition, he was a member of the American Philosophical Society, the National Academy of Sciences, and the New York Academy of the Arts and Sciences. Du Vigneaud's leisure interests included bridge and horse riding.

From 1967 to 1975, du Vigneaud served as Cornell University's professor of chemistry. In 1975 he advanced to the level of emeritus professor of biochemistry at Cornell. Du Vigneaud died at St. Agnes Hospital in White Plains, New York, on December 11, 1978.