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<title>Ralph Hirschmann</title>

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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Ralph Hirschmann</span></h1>

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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><p><b>Ralph Franz Hirschmann</b> (* <a href="6._Mai" title="6. Mai">6. Mai</a> <a href="1922" title="1922">1922</a> in <a href="F%C3%BCrth" title="Fürth">Fürth</a>; † <a href="20._Juni" title="20. Juni">20. Juni</a> <a href="2009" title="2009">2009</a> in <a href="Lansdale_(Pennsylvania)" title="Lansdale (Pennsylvania)">Lansdale</a>, <a href="Pennsylvania" title="Pennsylvania">Pennsylvania</a>) war ein US-amerikanischer <a href="Chemiker" title="Chemiker">Chemiker</a>.

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<div class="mw-heading mw-heading2"><h2 id="Leben_und_Werk">Leben und Werk</h2></div>

<p>Ralph F. Hirschmann wurde als Sohn von Carl und Alice Hirschmann, geb. Büchenbacher geboren. 1937 flohen sie aus Deutschland in die USA, wo er 1943 seinen <a href="Bachelor" title="Bachelor">Bachelor</a> am <a href="Oberlin_College" title="Oberlin College">Oberlin College</a> machte. Von 1943 bis 1946 leistete er seinen Dienst bei den <a href="Streitkr%C3%A4fte_der_Vereinigten_Staaten" title="Streitkräfte der Vereinigten Staaten">Streitkräften der Vereinigten Staaten von Amerika</a>. Anschließend machte er seinen <a href="Master" title="Master">Master</a> (1948) und <a href="Promotion_(Doktor)" title="Promotion (Doktor)">promovierte</a> (1950) bei William S. Johnson an der <a href="University_of_Wisconsin%E2%80%93Madison" title="University of Wisconsin–Madison">University of Wisconsin–Madison</a> mit der Arbeit <i>A new synthesis of the 6-methoxy-17-equilenones: some related stereochemical considerations, synthesis of 5-substituted-1-methyl-2-vinyl-1-cyclohexenes</i>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Dann wechselte er als pharmazeutischer Forscher zu <a href="Merck_%26_Co.%2C_Inc." class="mw-redirect" title="Merck & Co., Inc.">Merck & Co., Inc.</a>, wo er bald führender Kopf in der Protein- und <a href="Peptidmimetika" title="Peptidmimetika">Peptidmimetika</a>-Forschung wurde und mit seiner Gruppe viele Medikamente entwickeln konnte, darunter <a href="Lovastatin" title="Lovastatin">Mevacor</a>, <a href="Finasterid" title="Finasterid">Proscar</a>, <a href="Imipenem" title="Imipenem">Primaxin</a> und <a href="Ivermectin" title="Ivermectin">Ivermectin</a>. 1987 wurde er Forschungsprofessor an der <a href="University_of_Pennsylvania" title="University of Pennsylvania">University of Pennsylvania</a>. Daneben war er von 1987 bis 1999 Universitätsprofessor an der Medical University of South Carolina. Seit 1994 war er Makineni-Professor für bioorganische Chemie in Pennsylvania. 2006 wurde er <a href="Emeritierung" title="Emeritierung">emeritiert</a>.

</p><p>Hirschmann heiratete am 9. März 1951 Lucy Marguerite Aliminosa, mit der er zwei Kinder hatte: Ralph F. Hirschmann und Carla M. Hirschmann Hummel.

</p><p>Am 20. Juni 2009 starb Hirschmann mit 87 Jahren in Lansdale, Pennsylvania, USA.

</p><p>Ihm zu Ehren wird seit 1990 von der <a href="American_Chemical_Society" title="American Chemical Society">American Chemical Society</a> jährlich der <a href="Ralph_F._Hirschmann_Award_in_Peptide_Chemistry" title="Ralph F. Hirschmann Award in Peptide Chemistry">Ralph F. Hirschmann Award in Peptide Chemistry</a> für herausragende Beiträge auf dem Gebiet der Chemie der <a href="Peptide" class="mw-redirect" title="Peptide">Peptide</a> vergeben. Er wird von der Forschungsabteilung von Merck (<a href="MSD_Sharp_%26_Dohme" class="mw-redirect" title="MSD Sharp & Dohme">MSD Sharp & Dohme</a>) gefördert und ist mit 5.000 US-Dollar dotiert.

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<div class="mw-heading mw-heading2"><h2 id="Veröffentlichungen"><span id="Ver.C3.B6ffentlichungen"></span>Veröffentlichungen</h2></div>

<p>Hirschmann veröffentlichte mehr als 150 wissenschaftliche Arbeiten und war an nahezu 100 Patenten beteiligt.

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<ul><li>mit C. F. Hiskey und N. L. Wendler: <i>Rearrangement of the Steroid C/D Rings</i>. In: <i><a href="Journal_of_the_American_Chemical_Society" title="Journal of the American Chemical Society">Journal of the American Chemical Society</a></i>. Band 75, 1953, S. 5135.</li>

<li>mit N. G. Steinberg, P. Buchschacher, J. H. Fried, G. J. Kent, M. Tishler und S. L. Steelman: <i>Synthesis and Structure of Steroidal 4-Pregneno[3,2-c]-pyrazoles. A Novel Class of Potent Anti-Inflammatory Steroids</i>. In: <i>Journal of the American Chemical Society</i>. Band 85, 1963, S. 120–122.</li>

<li>mit R. G. Strachan, P. Buchschacher, L. H. Sarett, S. L. Steelman und R. Silber: <i>Approach to an Improved Anti-Inflammatory Steroid. Synthesis of 11β,17-Dihydroxy-3,20-dioxo-1,4-pregnadien-21-yl 2-Acetamido-2-deoxy-β-D-glucopyranoside</i>. In: <i>Journal of the American Chemical Society</i>. Band 86, 1964, S. 3903–3904.</li>

<li>mit R. F. Nutt, D. F. Veber, R. A. Vitali, S. L. Varga, T. A. Jacob, F. W. Holly, R. Denkewalter et al.: <i>Studies on the Total Synthesis of an Enzyme: I. Objective & Strategy; II. Synthesis of a Protected Tetratetracontapeptide Corresponding to the 21–64 Sequence of Ribonuclease A; III. Synthesis of a Protected Hexacontapeptide Corresponding to the 65–124 Sequence of Ribonuclease A; IV. Some Factors Affecting the Conversion of Protected S-Protein to Ribonuclease S'; V. The Preparation of Enzymatically Active Material.</i> In: <i>Journal of the American Chemical Society</i>. Band 91, 1969, S. 502–508.</li>

<li>mit D. F. Veber, F. W. Holly, W. J. Paleveda, R. F. Nutt, S. J. Bergstrand, M. L. Torchiana, M. S. Glitzer und R. Saperstein: <i>Conformationally Restricted Bicyclic Analogs of Somatostatin</i>. In: <i><a href="Proceedings_of_the_National_Academy_of_Sciences" class="mw-redirect" title="Proceedings of the National Academy of Sciences">Proceedings of the National Academy of Sciences</a></i>. Band 75, 1978, S. 2636–2640.</li>

<li>mit D. B. Smithrud, P. A. Benkovic, S. J. Benkovic, C. M. Taylor, K. M. Yager, J. Witherington, B. W. Phillips, P. A. Sprengeler und A. B. Smith, III: <i>Investigations of an Antibody Ligase</i>. In: <i>Journal of the American Chemical Society</i>. Band 119, 1997, S. 278–282.</li>

<li>mit A. B. Smith, III, A. Pasternak, W. Yao, P. A. Sprengeler, M. K. Holloway, L. C. Kuo, Z. Chen, P. L. Darke und W. A. Schleif: <i>An Orally Bioavailable Pyrrolinone Inhibitor of HIV-1 Protease: Computational Analysis and X-Ray Crystal Structure of the Enzyme Complex</i>. In: <i><a href="Journal_of_Medicinal_Chemistry" title="Journal of Medicinal Chemistry">Journal of Medicinal Chemistry</a></i>. Band 40, 1997, S. 2440–2444.</li>

<li>mit J. Hynes, Jr., M. A. Cichy-Knight, R. D. van Rijn, P. A. Sprengeler, P. G. Spoors, W. Shakespeare, S. Pietranico-Cole, J. Barbosa, W. Yao, S. Rohrer und A.B. Smith, III: <i>Modulation of Receptor and Receptor Subtype Affinities Using Diastereomeric and Enantiomeric Monosaccharide Scaffolds as a Means to Structural and Biological Diversity. A New Route to Ether Synthesis</i>. In: <i>Journal of Medicinal chemistry</i>. Band 41, 1998, S. 1382–1391.</li>

<li>mit J. Liu, D. Underwood, M. A. Cascieri, S. P. Rohrer, L-D. Cantin, G. Chicchi und A. B. Smith, III: <i>Synthesis of a Substance P Antagonist with a Somatostatin Scaffold: Factors Affecting Agonism/Antagonism at GPCRs and the Role of Pseudosymmetry</i>. In: <i>Journal of Medicinal chemistry</i>. Band 43, 2000, S. 3827–3831.</li>

<li>mit L. Abrous, J. Hynes, Jr., S. R. Friedrich und A. B. Smith, III: <i>Design and Synthesis of Novel Scaffolds for Drug Discovery: Hybrids of β-D-Glucose with 1,2,3,4-Tetrahydro-benzo[e][1,4]diazepin-5-one, the Corresponding 1-Oxazepine, and 2- and 4-Pyridyldiazepines</i>. In: <i>Organic letters</i>. Band 3, 2001, S. 1089–1092.</li>

<li>mit V. Prasad, E. T. Birzin, C. T. McVaugh, R. D. van Rijn, S. P. Rohrer, G. Chicchi, D. J. Underwood, E. R. Thornton, A. B. Smith, III: <i>Effects of Heterocyclic Aromatic Substituents on Binding Affinities at Two Distinct Sites of Somatostatin Receptors. Correlation with the Electrostatic Potential of the Substituents</i>. In: <i>Journal of Medicinal chemistry</i>. Band 46, 2003, S. 1858–1869.</li></ul>

<div class="mw-heading mw-heading2"><h2 id="Preise">Preise</h2></div>

<ul><li>1983 <a href="Alan_E._Pierce_Award" class="mw-redirect" title="Alan E. Pierce Award">Alan E. Pierce Award</a>, heute <a href="R._Bruce_Merrifield_Award" title="R. Bruce Merrifield Award">R. Bruce Merrifield Award</a> (<a href="American_Peptide_Society" title="American Peptide Society">American Peptide Society</a>)</li>

<li>1986 Medicinal Chemistry Award (<a href="American_Chemical_Society" title="American Chemical Society">American Chemical Society</a>)</li>

<li>1988 <a href="Nichols_Medal" class="mw-redirect" title="Nichols Medal">Nichols Medal</a></li>

<li>1992 <a href="Chemical_Pioneer_Award" title="Chemical Pioneer Award">Chemical Pioneer Award</a> (American Institute of Chemists)</li>

<li>1993 <a href="Max-Bergmann-Medaille" title="Max-Bergmann-Medaille">Max-Bergmann-Medaille</a></li>

<li>1993 Microbial Chemistry Medal (Kitasato Institute, Japan)</li>

<li>1994 <a href="Alfred_Burger_Award_in_Medicinal_Chemistry" title="Alfred Burger Award in Medicinal Chemistry">Alfred Burger Award in Medicinal Chemistry</a> (American Chemical Society)</li>

<li>1994 Carothers Award (American Chemical Society, Delaware Section)</li>

<li>1996 Padmavathy and Noth Guthikonda Memorial Award (<a href="Columbia_University" title="Columbia University">Columbia University</a>)</li>

<li>1996 <a href="Josef_Rudinger_Memorial_Award" title="Josef Rudinger Memorial Award">Josef Rudinger Memorial Award</a> (<a href="European_Peptide_Society" title="European Peptide Society">European Peptide Society</a>)</li>

<li>1996 Research Achievement Award in medical and natural product chemistry (American Association of Pharmaceutical Scientists)</li>

<li>1996 Club Award (Philadelphia Organic Chemists)</li>

<li>1999 National Academy of Sciences Award for the Industrial Application of Science</li>

<li>1999 <a href="Arthur_C._Cope_Award" title="Arthur C. Cope Award">Arthur C. Cope Award</a> (American Chemical Society)</li>

<li>1999 Edward E. Smissman Bristol Myers Squibb Award (American Chemical Society Division of Medicinal Chemistry)</li>

<li>2000 <a href="National_Medal_of_Science" title="National Medal of Science">National Medal of Science</a></li>

<li>2002 <a href="Willard_Gibbs_Medal" title="Willard Gibbs Medal">Willard Gibbs Medal</a> (American Chemical Society, Chicago Section)</li>

<li>2003 <a href="American_Institute_of_Chemists_Gold_Medal" title="American Institute of Chemists Gold Medal">American Institute of Chemists Gold Medal</a> (American Institute of Chemists)</li>

<li>2004 Mendel Medal (<a href="Villanova_University" title="Villanova University">Villanova University</a>)</li>

<li><a href="Ehrendoktor" title="Ehrendoktor">Ehrendoktorwürden</a>: 1969 Oberlin College, 1996 University of Wisconsin, Madison, 1997 Medical University of South Carolina</li></ul>

<div class="mw-heading mw-heading2"><h2 id="Mitgliedschaften">Mitgliedschaften</h2></div>

<ul><li>1981 <a href="American_Academy_of_Arts_and_Sciences" title="American Academy of Arts and Sciences">American Academy of Arts and Sciences</a></li>

<li>1999 <a href="National_Academy_of_Sciences" title="National Academy of Sciences">National Academy of Sciences</a></li>

<li>2001 Institute of Medicine</li>

<li><a href="American_Chemical_Society" title="American Chemical Society">American Chemical Society</a></li>

<li><a href="American_Association_for_the_Advancement_of_Science" title="American Association for the Advancement of Science">American Association for the Advancement of Science</a></li>

<li>American Society of Biological Chemists</li></ul>

<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>

<ul><li><i>Who’s Who in America</i>. 2007, S. 2031, ISBN 0-8379-7006-7</li>

<li>Dennis Hevesi: <a rel="nofollow" class="external text" href="https://www.nytimes.com/2009/07/19/science/19hirschmann.html"><i>Ralph F. Hirschmann, Leading Scientist on Early Enzyme Research, Dies at 87</i></a>. In: <i>The New York Times</i>. 18. Juli 2009</li></ul>

<div class="mw-heading mw-heading2"><h2 id="Weblinks">Weblinks</h2></div>

<ul><li>LA Times: <a rel="nofollow" class="external text" href="http://www.latimes.com/nation/la-me-ralph-hirschmann24-2009jul24-story.html">Ralph F. Hirschmann dies at 87; pioneering chemist</a> (englisch)</li>

<li><a rel="nofollow" class="external text" href="http://www.upenn.edu/almanac/between/Hirschmann.html">National Medal of Science: Ralph F. Hirschmann</a> (englisch)</li>

<li><a rel="nofollow" class="external text" href="http://astro4.ast.vill.edu/mendel/hirschmann.htm">Ralph Hirschmann 2004 Mendel Medal Recipient</a> (englisch)</li></ul>

<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>

<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://academictree.org/chemistry/peopleinfo.php?pid=53778">Informationen</a> zu und <a rel="nofollow" class="external text" href="https://academictree.org/chemistry/tree.php?pid=53778">akademischer Stammbaum</a> von <i>Ralph F. Hirschmann</i> bei academictree.org, abgerufen am 12. Februar 2018.<span class="editoronly" style="display:none;"></span></span>

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Normdaten (Person): <a href="Gemeinsame_Normdatei" title="Gemeinsame Normdatei">GND</a>: <span class="-print"><a rel="nofollow" class="external text" href="https://d-nb.info/gnd/139407294">139407294</a></span> | <a href="Library_of_Congress_Control_Number" title="Library of Congress Control Number">LCCN</a>: <span class="-print"><a rel="nofollow" class="external text" href="https://id.loc.gov/authorities/no2009103557">no2009103557</a></span> | <a href="Virtual_International_Authority_File" title="Virtual International Authority File">VIAF</a>: <span class="-print"><a rel="nofollow" class="external text" href="https://viaf.org/viaf/91125883/">91125883</a></span> | </div>

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