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Insulin at the German Wool Research Institute-Retrospect and Outlook

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Insulin & Related Proteins - Structure to Function and Pharmacology

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Abstract

This paper summarizes the research carried out between 1977 and 1999 in the German Wool Research Institute (Deutsches Wollforschungsinstitut, DWI) and in collaboration with other laboratories. Chemical synthesis and chemo-enzymatic semisynthesis yielded a large number of insulin analogues and special insulin probes, which allowed detailed structure-function studies and investigations based on photoaffinity labelling of insulin receptors. The outlook refers to some recent areas which are of potential interest for diabetes treatment and require further research.

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References

  • Albisser A.M. “Treatment of Diabetes Using Phosphorylated Insulin.” US Patent 5242900 (1993).

    Google Scholar 

  • Bota J. „Untersuchungen zum Faltungsweg monochenarer Insulinderivate.“ Thesis, RWTH Aachen (1999).

    Google Scholar 

  • Brandenburg D. and Wollmer A. (Eds.) “Insulin, Chemistry, Structure and Function of Insulin and Related Hormones.” Ed., Walter de Gruyter, Berlin, New York, (1980).

    Google Scholar 

  • Brandenburg D. “Insulin-structure, function, design.” Exp. Clin. Endocrinol. Diabetes 107, Suppl. 2 (1999): 6–12.

    Google Scholar 

  • Berndt, H. „Synthese der Sequenz 71–86 des Humanproinsulins, III. Synthese über die Fragmente 71–78 und 79–86.“ Hoppe-Seyler’s Z. Physiol. Chem. 360 (1979): 765–772

    PubMed  CAS  Google Scholar 

  • Bota J. „Untersuchungen zum Faltungsweg monochenarer Insulinderivate.“ Thesis, RWTH Aachen (1999).

    Google Scholar 

  • Brandenburg D. “Insulin-Structure, Function, Design.” Exp. Clin. Endocrinol. Diabetes 107, Suppl. 2 (1999): 6–12.

    Article  Google Scholar 

  • Brandenburg D. and Wollmer A. (Eds.) “Insulin, Chemistry, Structure and Function of Insulin and Related Hormones.” Ed., Walter de Gruyter, Berlin, New York, (1980).

    Google Scholar 

  • Brandenburg D., Fabry M., Pirrwitz J., Strack U., Thevis W., Wittkamp A., Schaefer E., Ellis L., Keana J.E. and Cai S.X.. “Novel Derivatives for Analyzing the Interaction between Insulin and its Receptor.” In: Peptides 1992 (Schneider C.H. and Eberle, A.N. eds.) Escom Science Publishers B.V., Leiden, (1993): pp 111–112.

    Google Scholar 

  • Brandenburg, D., Diaconescu, C., Saunders, D. and Thamm, P. “Covalent Linking of Photoreactive Insulin to Adipocytes Produces a Prolonged Signal.” Nature 286 (1980a): 821–822.

    Article  PubMed  CAS  Google Scholar 

  • Brandenburg, D., Lei, K., Wang, Z., Dong, B., Binggen, R. and Zhu, S.: “Preparations and Properties of Crystalline Porcine and Bovine (Trp) B1 Insulins.” Scientia Sinica 23, 1443–1452 (1980b).

    CAS  Google Scholar 

  • Büllesbach E.E. “Semisynthesis of a Shortened Open-Chain Proinsulin.” Tetrahedron Letters 23 (1982): 1877–1880.

    Google Scholar 

  • Büllesbach, E.E. and Naithani, V.K. „Semisynthesen, ausgehend von Proinsulin, II. Darstellung und Anwendung von Nσ 29, Nσ 59 -Bis(methylsulfonethoxy-carbonyl)-proinsulin.“ Hoppe-Seyler’s Z. Physiol. Chem. 361 (1980): 723–734.

    PubMed  Google Scholar 

  • Büllesbach, E.E., Danho, W., Helbig, H.-J. and Zahn, H. “Human Proinsulin, VIII. Studies on the S-Tritylation of Reduced Proinsulin, Insulin A and B Chains and their Detritylation.” Hoppe-Seyler’s Z.Physiol.Chem. 361 (1980): 865–873.

    PubMed  Google Scholar 

  • Casaretto M., Spoden M., Diaconescu C., Gattner H.-G., Zahn H., Brandenburg D. and Wollmer A. “Shortened Insulins with Enhanced in vitro Potency.” Biol Chem. Hoppe-Seyler 368 (1987): 709–716.

    PubMed  CAS  Google Scholar 

  • Casaretto R. „Merrifieldsynthese von [A1a12]-und [Ile12]Insulin-B-Ketten und Kombination mit natürlicher A-Kette.“ Thesis, RWTH Aachen (1986).

    Google Scholar 

  • Chu, S.-C., Wang, C.-C and Brandenburg, D. “Preparation and Properties of Des-pentapeptide(B26-30)-Insulin Analogues.” In Brunfeldt, K. (Ed.) Peptides 1980, Proceedings. of the Sixteenth European Peptide Symposium. The Danish Institute of Protein Chemistry, Copenhagen, 1981a, pp. 359–364.

    Google Scholar 

  • Chu S., Wang, C. and Brandenburg D. “Intramolecular Enzymatic Peptide Synthesis: Trypsin-mediated Coupling of the Peptide Bond between B22-Arginine and B23-Glycine in a Split Crosslinked Insulin.” Hoppe-Seyler’s Z. Physiol. Chem. 362 (1981b): 647–654.

    PubMed  CAS  Google Scholar 

  • Cutfield S.M., Dodson G.G., Schwertner E. and Zahn H. “X-Ray Diffraction of Crystals of Half-Synthetic Sheep Insulin.” Hoppe-Seyler’s Z. Physiol Chem. 360 (1979): 783–785.

    PubMed  CAS  Google Scholar 

  • Danho, W. and Föhles, J. “Human Proinsulin, IV. Synthesis of a Protected Peptide Fragment Corresponding to the Sequence 1–23 of the Prohormone.” Hoppe-Seyler’s Z.Physiol.Chem. 361 (1980): 839–847

    PubMed  CAS  Google Scholar 

  • Danho, W., Naithani, V.K., Sasaki, A.N., Föhles, J., Berndt, H., Büllesbach, E.E. and Zahn, H. “Human Proinsulin, VII. Synthesis of Two Protected Peptides Corresponding to the Sequences 1–45 and 46–86 of the Prohormone.” Hoppe-Seyler’s Z.Physiol.Chem. 361 (1980a): 857–863.

    PubMed  CAS  Google Scholar 

  • Danho, W., Sasaki, A., Büllesbach, E., Föhles, J. and Gattner, H.-G. “[A19-Phenylalanine]Insulin: A New Synthetic Analogue.” Hoppe-Seyler’s Z. Physiol. Chem. 361 (1980b): 735–746.

    PubMed  CAS  Google Scholar 

  • Danho W., Sasaki A., Büllesbach E., Gattner H.-G. and Wollmer A. “[A14]-Phenylalanine] Insulin: A New Synthetic Analogue.” Hoppe-Seyler’s Z. Physiol. Chem. 361 (1980c): 747–754.

    PubMed  CAS  Google Scholar 

  • Diaconescu C., Saunders D., Gattner H.-G. and Brandenburg D. “[LeuB24]-and [LeuB25]Insulins are not Antagonists of Lipogenesis in Adipocytes.” Hoppe Seyler’s Z. Physiol. Chem. 363 (1982): 187–192.

    PubMed  CAS  Google Scholar 

  • Fabry M. “Synthesis and Characterization of Photoreactive Insulin-like Growth Factor 1 Derivatives for Receptor Analysis.” Bioconjugate Chem. 10 (1999): 200–205.

    Article  CAS  Google Scholar 

  • Fabry M., Schaefer E., Ellis L., Kojro E., Fahrenholz F. and Brandenburg D. “Detection of a New Hormone Contact Site within the Insulin Receptor Ectodomain using a Novel Photoreactive Insulin.” J. Biol. Chem. 267 (1992): 8950–8956.

    PubMed  CAS  Google Scholar 

  • Fabry, M. and Brandenburg, D. “Design and Synthesis of a Novel Biotinylated Photoreactive Insulin for Receptor Analysis.” Biochemistry Hoppe-Seyler 373 (1992a):143–150.

    CAS  Google Scholar 

  • Fabry, M. and Brandenburg, D. “Analysis of the Human Placental Insulin Receptor.” Biochemistry Hoppe-Seyler 373 (1992b): 915–923.

    CAS  Google Scholar 

  • Fischer W.H., Saunders D., Brandenburg D., Wollmer A. and Zahn H. “A Shortened Insulin with Full in vitro Potency.” Biol. Chem. Hoppe-Seyler 366 (1985): 521–525.

    PubMed  CAS  Google Scholar 

  • Fischer, W.H., Saunders, D., Brandenburg, D., Diaconescu, C., Wollmer, A., Dodson, G., De Meyts, P. and Zahn, H. “Structure-Function Relationships of Shortened (LeuB25) Insulins, Semisynthetic Analogues of a Mutant Human Insulin.” Biol. Chem. Hoppe-Seyler 367(1986): 999–1006

    PubMed  CAS  Google Scholar 

  • Friesen, H.-J., Naithani, V.K. and Gattner, H.-G. “Preparation and Application of N α -B1,N εl -B29-Bis(tert.-butyloxycarbonyl)insulin.” Hoppe-Seyler’s Z. Physiol. Chem. 359 (1978): 103–111.

    PubMed  CAS  Google Scholar 

  • Gattner H.-G., Danho W. und Naithani V.K. “Enzyme-catalyzed Semisynthesis with Insulin Derivatives.” In: Insulin, Chemistry, Structure and Function of Insulin and Related Hormones, Ed. (D. Brandenburg, A. Wollmer, Walter de Gruyter, Berlin, New York, (1980a): 117–123.

    Google Scholar 

  • Gattner H.-G., Danho W., Behn C. and Zahn H.. “The Preparation of Two Mutant Forms of Human Insulin, Containing Leucine in Position B24 or 25, by Enzyme-Assisted Synthesis.” Hoppe-Seyler’s Z. Physiol. Chem. 361 (1980b): 1135–1138.

    PubMed  CAS  Google Scholar 

  • Gattner H.-G., Krail G., Danho W., Knorr R., Wieneke H.-J., Buellesbach E.E., Schartmann B., Brandenburg D. and Zahn H.. „Eine verbesserte Methode der Kombination von Insulinketten zur Darstellung von Insulinanalogen.“ Hoppe-Seyler’s Z. Physiol. Chem. 362 (1981): 1043–1049.

    PubMed  CAS  Google Scholar 

  • Gattner, H.-G. and Naithani, V.K. “C-Terminal Carboxyl Function (Thr-B3O) Mediated Cross-Linking and Immobilization of Insulin.” In Jung, G. and Bayer, E. (Eds.) Peptides. Walter de Gruyter, Berlin, New York, 1989, pp. 262–264.

    Google Scholar 

  • Gattner, H.-G. and Schmitt, E.W. “(A21-Asparaginimide) Insulin. Saponification of Insulin Hexamethyl Ester, I.” Hoppe-Seyler’s Z. Physiol. Chem. 358 (1977) 105–113.

    PubMed  CAS  Google Scholar 

  • Havenith C. „Neue kovalente Insulindimere: Semisynthese und biologische Eigenschaften.“ Thesis RWTH Aachen (1999).

    Google Scholar 

  • Havenith C. and Brandenburg D. „Kovalent verbrückte Insulindimere.“ DOS (31.8.2000) DE 19908041 A1 (2000).

    Google Scholar 

  • Höcker H., Brandenburg D., Lenz V. and Kleinjung J. „Phosphorylierte Insuline und deren Derivate, Verfahren zu deren Herstellung, ihre Verwendung und eine sie enthaltende Zubereitung.“ DOS DE 195 35 701 A1 (1997).

    Google Scholar 

  • Jonczyk A. and Gattner H.-G. „Eine neue Semisynthese des Humaninsulins-Tryptisch-katalysierte Transpeptidierung von Schweineinsulin mit L-Threonin-tert-butylester.“ Hoppe-Seyler’s Z. Physiol. Chem. 362(1981): 1591–1598.

    PubMed  CAS  Google Scholar 

  • Jonczyk, A., Keefer, L.M., Naithani, V.K., Gattner, H.-G., De Meyts, P. and Zahn, H. “Preparation and Biological Properties of [LeuB24, LeuB25] Human Insulin.” Hoppe-Seyler’s Z. Physiol. Chem. 362 (1981)557–561.

    PubMed  CAS  Google Scholar 

  • Jones R.H., Shojaee-Moradi F., Sönksen P.H., Brandenburg D., Schüttler A. and Eckey H. “Hepatoselective Pharmaceutical Actives.” USP 6063761 (2000).

    Google Scholar 

  • King G.L., Kahn C.R., Samuels B., Danho W., Büllesbach E.E. and Gattner, H.G. “Synthesis and Characterization of Molecular Hybrids of Insulin and Insulin-like Growth Factor I. The Role of the A-chain Extension Peptide.” Biol. Chem. 257 (1982): 10869–10873.

    CAS  Google Scholar 

  • Klotz, G., Saunders, D.J. and Brandenburg, D. “The Biological Potency of Covalent Insulin-Receptor Complexes: Dependence on Site of Cross-linkage.” Hoppe-Seyler’s Z. Physiol. Chem. 365 (1984a) 493–498.

    PubMed  CAS  Google Scholar 

  • Klotz, G., Saunders, D. and Brandenburg, D. “Biological Potency of Covalently Linked Insulin-Receptor in Rat Adipocyte. Comparison with the Potency of Reversible Complexes.” Biochim. Biophys. Acta 803 (1984b) 78–84

    PubMed  CAS  Google Scholar 

  • Knorr R., Danho W., Büllesbach E.E., Gattner H.-G., Zahn H., King G.L. and Kahn C.R. “[B22-D Arginine]Insulin: Synthesis and Biological Properties.” Hoppe-Seyler’s Z. Physiol. Chem. 363 (1982): 1449–1460.

    PubMed  CAS  Google Scholar 

  • Knorr, R., Danho, W., Büllesbach, E.E., Gattner, H.G., Zahn, H., King, G.L. and Kahn, C.R. “[B17-D Leucine]Insulin and [B17-Norleucine]Insulin: Synthesis and Biological Properties.” Hoppe Seyler’s Z. Physiol. Chem. 364 (1983): 1615–1626.

    PubMed  CAS  Google Scholar 

  • Kurapkat G., Siedentop M., Gattner H.-G., Hagelstein M., Brandenburg D., Grötzinger J. and Wollmer A. “The Solution Structure of a Superpotent B-chain-shortened Single-replacement Insulin Analogue.” Protein Sci. 8 (1999): 499–508.

    PubMed  CAS  Google Scholar 

  • Kurapkat, G., De Wolf, E., Grötzinger, J. and Wollmer, A. “Inactive Conformation of an Insulin Despite its Wild-type Sequence.” Protein Sci 6. (1997): 580–587.

    PubMed  CAS  Google Scholar 

  • Lauter S. „Phosphorylierte Insulin-Hybride mit Affinität zu Plasmaproteinen.“ Thesis RWTH Aachen (1999).

    Google Scholar 

  • Lenz V., Gattner H.-G., Seivert D., Wollmer A., Engels M. and Höcker H. “Semisynthetic Des-(B27-B30)-insulins with Modified B26-Tyrosine.” Biol. Chem. Hoppe-Seyler 372 (1991): 495–504.

    PubMed  CAS  Google Scholar 

  • Lenz V., Leithäuser M., Casaretto M., Gattner H.-G., Brandenburg D. and Höcker H. “An Enzymatic chemical Synthesis of Insulins with Non-proteinogenic Amino Acid Residues via Chain Condensation and Subsequent Disulfide Folding.” In: Peptides: Chemistry, Structure and Biology. Eds.: (P.T.P. Kaumaya, R.S. Hodges, Mayflower Scientific Ltd., (1996): 637–638.

    Google Scholar 

  • Lenz V.J., Federwisch M., Gattner H.-G., Brandenburg D., Höcker H., Hassiepen U. and Wollmer A. “Structure and Rotational Dynamics of Fluorescently Labeled Insulin in Aqueous Solution and at the Amphiphile-Water Interface of Reversed Micelles.” Biochemistry 34 (1995): 6130–6141.

    Article  PubMed  CAS  Google Scholar 

  • Lenz V.J., Gattner H.-G., Leithäuser M., Brandenburg D., Wollmer A. and Höcker H. “Proteolysis of a Fluorogenic Insulin Derivative and Native Insulin in Reversed Micelles Monitored by Fluorescence Emission, Reversed-phase High-performence Liquid Chromatography, and Capillary Zone Electrophoresis.” Anal. Biochem. 221 (1994): 85–93.

    Article  PubMed  CAS  Google Scholar 

  • Leyer S., Gattner H.-G., Leithäuser M., Brandenburg D., Wollmer A. and Höcker H. “The Role of the C-terminus of the Insulin B-chain in Modulating Structural and Functional Properties of the Hormone.” Int. J. Peptide Protein Res. 46 (1995): 397–407.

    CAS  Google Scholar 

  • Mucke, P., Diaconescu, C., Klotz, G., Jorgensen, P., Saunders, D. and Brandenburg, D. “Recognition of Covalent Insulin-Receptor Complexes on Viable Adipocytes by Anti-insulin Antibodies.” Biol. Chem. Hoppe-Seyler 368 (1987) 85–92.

    PubMed  CAS  Google Scholar 

  • Naithani V.K. and Zahn H. “Synthesis of Proinsulin.” Peptide and Protein Reviews 3, Ed. (Milton T.W. Hearn, Marcel Dekker, Inc., New York and Basel (1984).

    Google Scholar 

  • Naithani, V.K. and Gattner, H.G. “Preparation and Properties of Citraconyl-insulins.” Hoppe-Seyler’s Z. Physiol. Chem. 363, 1443–1448 (1982)

    PubMed  CAS  Google Scholar 

  • Naithani, V.K. and Schwertner, E. “Human Proinsulin VI. Synthesis of Protected Segment 46–70 of Prohormone.” Hoppe Seyler’s Z. Physiol. Chem. 364(1983), 1603–1613

    PubMed  CAS  Google Scholar 

  • Naithani, V.K., Büllesbach, E.E. and Zahn, H. “Semisynthesis of a Des-(1-21)-Preproinsulin Derivative.” Hoppe-Seyler’s Z. Physiol. Chem. 360 (1979) 1363–1366.

    PubMed  CAS  Google Scholar 

  • Neffe J. „Struktur und Internalisierung des Insulinrezeptors“. Thesis, RWTH Aachen (1985).

    Google Scholar 

  • Sasaki, N.A. “Synthesis of Human Proinsulin Sequence 71–86, II. Improved Synthesis of the Fragment.” Hoppe-Seyler’s Z.Physiol.Chem. 360 (1979) 761–764.

    PubMed  CAS  Google Scholar 

  • Saunders D. and Freude K. “Cross-Linked [DalaA1]Insulins. Evidence for a Change in the Conformation of the Insulin Monomer at its Receptor.” Hoppe Seyler’s Z. Physiol. Chem. 363 (1982): 655–659.

    PubMed  CAS  Google Scholar 

  • Saunders D., Klotz G. and Brandenburg D. “Biological Activity of Covalently-linked Insulin-receptor Complexes in Rat Adipocytes. Effect of pH.” Biochim. Biophys. Acta 803 (1984): 85–89.

    PubMed  CAS  Google Scholar 

  • Saunders D.J. and Brandenburg D. “Iodinated A1-NY-(4-Azidophenylacetyl)-D-α,γ-diaminobutyric acid Insulin: Its Preparation and Properties.” Hoppe-Seyler’s Z. Physiol. Chem. 362 (1981): 1237–1245.

    PubMed  CAS  Google Scholar 

  • Saunders, D., Freude, K., Naithani, V.K., Brandenburg, D. and Stoev, S. “Semisyntheses of Insulin Analogues by Replacement of the Sequence A 1–4.” In Blaha, K. and Malon, P. (Eds.) Peptides 1982. Walter de Gruyter & Co., Berlin-New York, 1983, pp. 371–374.

    Google Scholar 

  • Schartmann, B., Gattner, H.-G., Danho, W. and Zahn, H. „Erhöhte Insulinausbeuten durch “Recycling” der nicht-kombinierten Ketten.“ Hoppe-Seyler’s Z. Physiol. Chem. 364 (1983), 179–186.

    PubMed  CAS  Google Scholar 

  • Schmitt, W.E. and Gattner, H.-G. „Verbesserte Darstellung von Des-alanylB30-insulin“ Hoppe-Seyler’s Z. Physiol. Chem. 359 (1978): 799–802.

    PubMed  CAS  Google Scholar 

  • Schumacher R., Soos M.A., Schlessinger J., Brandenburg D., Siddles K. and Ullrich A. “Signaling competent Receptor Chimeras Allow Mapping of Major Insulin Receptor Binding Domain.” J. Biol. Chem. 268 (1993): 1087–1094.

    PubMed  CAS  Google Scholar 

  • Schüttler A. and Brandenburg, D. “Preparation and Properties of Covalently Linked Insulin Dimers.” Hoppe-Seyler’s Z. Physiol. Chem. 363 (1982): 317–330.

    PubMed  Google Scholar 

  • Schüttler A., Diaconescu C., Saunders D.J. and Brandenburg D. “Time-dependence of Biological Activity Induced by Covalent Insulin-receptor Complexes in Rat Adipocytes.” Biochem. J. 232 (1985): 49–53.

    PubMed  Google Scholar 

  • Schüttler, A. and Brandenburg, D. „Darstellung von N, N-Bis(methylsulfonyl-ethoxycarbonyl) insulinen.“ Hoppe-Seyler’s Z.Physiol.Chem. 360 (1979) 1721–1725.

    PubMed  Google Scholar 

  • Shojaee-Moradie F., Eckey H., Jackson N.C., Schüttler A., Brandenburg D., Sönksen P.H. and Jones R.H. “Novel Hepatoselective Insulin Analogues: Studies with Covalently Linked Thyroxylinsulin Complexes.” Diabet. Med. 15 (1998): 928–936.

    Article  PubMed  CAS  Google Scholar 

  • Siedentop M. „Erhöhung der Segmentflexibilität im Rezeptorbindungsbereich B23-B26 des Insulins.” Thesis, RWTH Aachen (1997).

    Google Scholar 

  • Sievert D. „Semisynthese und Struktur-Funktionsuntersuchung von Des-Tetrapeptid(B27-B30)-Insulinen mit Austausch von B26-Tyrosin.” Thesis, RWTH Aachen (1991).

    Google Scholar 

  • Sievert D., Lenz V., Gattner H.-G., Brandenburg D., Höcker H. and Wollmer A. “Residue B26 Modulates Structural and Functional Properties of Des(B27-B30)-insulin.” In: Chemistry of Peptides and Proteins (D. Brandenburg, V. Ivanov, W. Voelter, eds.) Vol. 5/6 DWI Reports 112B Aachen (1993): pp 425–431.

    Google Scholar 

  • Spoden M., Gattner H.-G., Zahn H. and Brandenburg D. “Structure-Function Relationship of Des-(B26-B30)-insulin.” Int. J. Peptide Protein Res. 46 (1995): 221–227.

    CAS  Google Scholar 

  • Stoev S., Zakhariev S., Golovinsky E., Gattner H.-G., Naithani V. K., Wollmer A. and Brandenburg D. “Synthesis and Properties of A19-(p-Fluorophenylalanine) Insulin.” Biol. Chem. Hoppe-Seyler 369 (1988): 1307–1315.

    PubMed  CAS  Google Scholar 

  • Sundermann E. „Heteromere Insulin-Hybride mit Affinität zu Plasmaproteinen.“ Thesis RWTH Aachen (1999).

    Google Scholar 

  • Svoboda, I., Brandenburg, D., Barth, T., Gattner, H.-G., Jiracek, J., Velek, J., Blaha, I., Ubik., K., Kasicka., V., Pospisek., J. and Hrbas, P. “Semisynthetic Insulin Analogues Modified in Position B24, B25 and B29.” Biochemistry Hoppe-Seyler 375 (1994) 373–378

    CAS  Google Scholar 

  • Thamm P., Saunders D. and Brandenburg D. “Photoreactive Insulin Derivatives: Preparation and Characterization.” In: Insulin, Chemistry, Structure and Function of Insulin and Related Hormones, Ed. (D. Brandenburg, A. Wollmer, Walter de Gruyter, Berlin, New York (1980): 309–316.

    Google Scholar 

  • Trindler, P. and Brandenburg, D. “Semisynthetic Modification of the N-terminus of the Insulin-A-chain.” In Chemistry of Peptides and Proteins 1, Walter de Gruyter & Co., Berlin-New York, 1982, pp. 308–314.

    Google Scholar 

  • Videnov G., Buettner K., Casaretto M., Foehles J., Gattner H.-G., Stoev S. and Brandenburg D. “Studies on the Total Synthesis of an A7,B7-Dicarba-Insulin, III. Assembly of Segments and Generation of Biological Activity.” Biol. Chem. Hoppe-Seyler 371 (1990): 1057–1066.

    PubMed  CAS  Google Scholar 

  • Weber J. „Synthese und Rückfaltungsstudien von verbrückten Insulinen mit Aminosäureaustausch in den Positionen A3 und B15.“ Thesis, RWTH Aachen (1998).

    Google Scholar 

  • Wedekind F., Baer-Pontzen K., Bala-Mohan S., Choli D., Zahn H. and Brandenburg D. “Hormone Binding Site of the Insulin Receptor: Analysis Using Photoaffinity-mediated Avidin Complexing.” Biol. Chem. Hoppe-Seyler 370 (1989): 251–258.

    PubMed  CAS  Google Scholar 

  • Weiland M., Brandenburg C., Brandenburg D. and Joost H.G. “Antagonistic Effects of a Covalently Dimerized Insulin Derivative on Insulin Receptors in 3T3-L1 Adipocytes.” Proc. Natl. Acad. Sci. USA 87 (1990): 1154–1158.

    PubMed  CAS  Google Scholar 

  • Weimann H.-J. „Partialsynthese von Insulinanalogen mit modifiziertem N-Terminus der B-Kette”. Thesis, RWTH Aachen (1977).

    Google Scholar 

  • Weitzel G. „Insulinforschung im Deutschen Wollforschungsinstitut an der RWTH Aachen“. In: Festschrift zum 25jährigen Jubiläum. Zahn, H. and Ziegler, K. (Eds.) Deutsches Wollforschungsinstitut Aachen, Aachen (1977): pp. 439–476.

    Google Scholar 

  • Wieneke H.J., Danho W., Büllesbach E., Gattner H.G. and Zahn H. “The Synthesis of [A19-3-Iodotyrosine] and [A19-3,5-Diiodotyrosine] insulin (porcine).” Hoppe-Seyler’s Z. Physiol Chem. 364 (1983): 537–550.

    PubMed  CAS  Google Scholar 

  • Wolf G., Berndt H. and Brandenburg D. „Synthese der [Lys A13] Rinderinsulin-A-Kette in der Form [Lys(Tfa)A13]A(SO3H)4 und Nα-Msc-[LysA13]A(SO3H)4 unter Verwendung des S-tert-Butylmercapto-Restes als Thiolschutz.” Hoppe-Seyler’s Z. Physiol. Chem. 360 (1979): 1569–1578.

    PubMed  CAS  Google Scholar 

  • Wollmer A., Gilge G., Brandenburg D. and Gattner H.-G. “An Insulin with the Native Sequence but Virtually no Activity.” Biochemistry Hoppe-Seyler 375 (1994): 219–222.

    CAS  Google Scholar 

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  1. D. Brandenburg
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Editors and Affiliations

  1. Novo Nordisk Pharma GmbH, Mainz, Germany

    Markus Leyck Dieken

  2. Institut für Biochemie, RWTH, Aachen, Germany

    Matthias Federwisch

  3. Hagedorn Research Laboratory, Gentofte, Denmark

    Pierre De Meyts

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Brandenburg, D. (2002). Insulin at the German Wool Research Institute-Retrospect and Outlook. In: Dieken, M.L., Federwisch, M., De Meyts, P. (eds) Insulin & Related Proteins - Structure to Function and Pharmacology. Springer, Dordrecht. https://doi.org/10.1007/0-306-47582-0_2

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  • DOI: https://doi.org/10.1007/0-306-47582-0_2

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