Aphrodite Kapurniotu: CIPSM-Professorship for peptide biochemistry



Born May 3, 1961 in Larisa, Greece


Education, Training, Positions

1979-1985 Diploma Studies in Chemistry at the University of Athens and the University of Tübingen

1986-1990 PhD Studies in Peptide Chemistry, supervisor Prof. Dr. W. Voelter, University of Tübingen

1990 PhD Degree, Faculty of Chemistry and Pharmacy, University of Tübingen

1990-1992 Research and Teaching Assistant, University of Tübingen

1992-1994 Postdoctoral Investigator with Prof. J. W. Taylor, Department of Chemistry, Rutgers University, NJ, USA

1994-1995 Senior Scientist with Prof. A. Cerami and Prof. R. Bucala, Picower Institute for Medical Research, NY, USA

1995-2002 Group Leader “Molecular Peptide Research” (Hochschulassistentin), University of Tübingen

2001 Habilitation in Biochemistry, Faculty of Chemistry and Pharmacy, University of Tübingen

2002 Group Leader “Molecular Mechanisms of Protein Aggregation Diseases” (Oberassistentin), Hospital of Psychiatry and Psychotherapy, University Hospital Tübingen

2002-2007 Group Leader “Bioorganic and Medicinal Chemistry” and Privatdozentin, Institute of Biochemistry, University Hospital RWTH Aachen

2006 apl. Professor, Biochemistry, RWTH Aachen

Since Oct. 2007 Professor, Peptide Biochemistry, TU München


Research Interests

Our research aims at understanding biomolecular interactions of proteins and polypeptides involved in biological and disease-associated processes via chemistry and at developing novel molecular strategies, compounds, and chemical tools to intervene with these processes.

We are especially interested in understanding biomolecular recognition, biological function, and molecular processes linked to disease associated cell toxicity of proteins and polypeptides, using protein(peptide) chemical design and synthesis strategies and in designing peptide-based compounds as agonists, antagonists, modulators, competitors, or inhibitors of the above processes and related biological or disease associated effects. 

Current research activities focus on: 

-- understanding protein misfolding, protein/protein interactions, biomolecular recognition, self-assembly, amyloidogenesis, and gain-of-cell toxicity molecular events underlying cell degeneration and pathogenesis of the protein aggregation diseases Alzheimer`s disease (AD) and type II diabetes (T2D) and

-- designing/developing novel molecular strategies to interfere with protein misfolding, aggregation, and cell degeneration and to generate therapeutic compounds and non-invasive diagnostic tools in AD and T2D. 



Prof. Dr. Aphrodite Kapurniotu

Department of Biosciences

Laboratory of Peptide Biochemistry

Technische Universität München

An der Saatzucht 5

85350 Freising-Weihenstephan


Phone: +49 8161 713542

Fax: +49 8161 713298

Email: akapurniotu@wzw.tum.de





1. “Cytotoxicity of Insulin within its Self-assembly and Amyloidogenic Pathways” S. Grudzielanek, A. Velkova, A. Shukla, V. Smirnovas, M. Tatarek-Nossol, H. Rehage, A. Kapurniotu, Winter R. J. Mol. Biol., 370, 372-84 (2007).

2. “Designed IAPP Mimic Blocks Ab Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Ab and IAPP Suggests a Molecular Link between Alzheimer’s Disease and Type 2 Diabetes” L.-M. Yan, A. Velkova, M. Tatarek-Nossol, E. Andreetto, A. Kapurniotu Angew. Chem. Int. Ed. Engl. 46, 1246-1252 (2007).

3.  “Design of a mimic of non-amyloidogenic and bioactive IAPP as a nanomolar affinity inhibitor of IAPP fibrillogenesis and cytotoxicity” L.-M. Yan, M. Tatarek-Nossol, A. Velkova, A. Kazantzis, A. Kapurniotu Proc. Natl. Acad. Sci. USA, 103, 2046-2051 (2006).

4. "A novel drug-eluting stent coated with an integrin-binding cRGD peptide inhibits neointimal hyperplasia by recruiting endothelial progenitor cells" R. Blindt, F. Vogt, I. Astafieva, C. Fach, N. Krott, B. Seitz,  A. Kapurniotu, C. Kwok, M. Dewor, M. Hristov,  A. Bosserhoff,  J. Bernhagen, P. Hanrath, R. Hoffmann, C. WeberJ. Am. Coll. Cardiol. 47, 1786-95 (2006).

5. “Rapid and transient activation of the ERK MAPK signalling pathway by macrophage migration inhibitory factor (MIF) and dependence on JAB1/CSN5 and Src kinase activity” H. Lue, A. Kapurniotu, G. Fingerle-Rowson, T. Roger, L. Leng, M. Thiele, T. Calandra, R. Bucala, J. Bernhagen Cell Signal., 18, 688-703 (2005).

6. “Macrophage migration inhibitory factor (MIF) increases neuronal delayed rectifier K+ current” T. Matsuura, C. Sun, L. Leng, A. Kapurniotu, J. Bernhagen, R. Bucala, A. E. Martynyuk, C. Sumners J. Neurophysiol., 95, 1042-1048 (2005).

7. “Inhibition of IAPP amyloid fibril formation and apoptotic cell death by a designed IAPP amyloid core-containing hexapeptide”, M. Tatarek-Nossol, L.M. Yan, A. Schmauder, K. Tenidis, G. Westermark A. Kapurniotu Chem. Biol., 12, 797-809 (2005).

8. “Targeting a-synuclein in Parkinson’s disease”, A. Kapurniotu Chem. Biol., 11, 1476-77 (2004) (Preview).

9. “Contribution of conformationally constrained calcitonin analogues to the understanding of the structural and conformational requirements of calcitonin bioactivity and to the design of potent agonists”, A. Kapurniotu Curr. Med. Chem., 11, 2577-97 (2004) (Review).

10. A sixteen residue peptide fragment of macrophage migration inhibitory factor, MIF(50-65), exhibits redox activity and has MIF-like biological functions”, M. T. Nguyen, J. Beck, H. Lue, R. Kleemann, P. Koolwijk, A. Kapurniotu, J. Bernhagen. J. Biol. Chem. 278, 33654-71 (2003).

11. “Conformational restriction via cyclization in b-amyloid peptide Ab(1-28) leads to an inhibitor of Ab(1-28) amyloidogenesis and cytotoxicity”, A. Kapurniotu, A. Buck, M. Weber, A. Schmauder, T. Hirsch, J. Bernhagen, M. Tatarek-Nossol. Chem. Biol. 10, 149-159 (2003).

12. „Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity”, A. Kapurniotu, A. Schmauder, K. Tenidis. J. Mol. Biol., 315, 339-350 (2002).

13. „Side-chain lactam-bridge conformational constrains differentiate the activities of salmon and human calcitonins and reveal a new design concept for potent calcitonin analogues“, J. W. Taylor, Q. K. Jin, M. Sbacchi, L. Wang, P. Belfiore, M. Garnier, A. Kazantzis, A. Kapurniotu, P. F. Zaratin, M. A. Scheideler. J. Med. Chem., 45, 1108-1121 (2002).

14. „Conformationally constrained human calcitonin (hCt) analogues reveal a critical role of sequence 17-21 for the oligomerization state and bioactivity of hCt“, A. Kazantzis, M. Waldner, J. W. Taylor, A. Kapurniotu. Eur. J. Biochem., 269, 780-791 (2002).

15. „Amyloidogenicity and cytotoxicity of islet amyloid polypeptide (IAPP)“, A. Kapurniotu. Biopolymers, 60, 438-59 (2001) (Review).

16. „Amyloidogenicity of recombinant human pro-islet amyloid polypeptide (ProIAPP)“, M. Krampert, J. Bernhagen, J. Schmucker, A. Horn, A. Schmauder, H. Brunner, W. Voelter, & A. Kapurniotu. Chem. Biol., 7, 855-871 (2000).

17. „Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1“, R. Kleemann, A. Hausser, G. Geiger, R. Mischke, A. Burger-Kentischer, O. Flieger, F.-J. Johannes, T. Roger, T. Calandra, A. Kapurniotu, M. Grell, D. Finkelmeier, H. Brunner, & J. Bernhagen. Nature, 408, 211-216 (2000).

18. „Activated protein C inhibits tumor necrosis factor and macrophage migration inhibitory factor (MIF) production in monocytes“, M. Schmidt-Supprian, C. Murphy, B. White, M. Lawler, A. Kapurniotu, W. Voelter, O. Smith, J. Bernhagen. Eur. Cytokine Netw., 11, 3 (2000).

19. „Identification of a Penta- and Hexapeptide of Islet Amyloid Polypeptide (IAPP) with Amyloidogenic and Cytotoxic Properties“, K. Tenidis, M. Waldner, J. Bernhagen, W. Fischle, M. Bergmann, M. Weber, M.-L. Merkle, W. Voelter, H. Brunner, A. Kapurniotu, J. Mol. Biol., 295, 1055-1071 (2000).

20. „Rational design, confomational studies and bioactivity of novel, highly potent, conformationally constrained calcitonin analogues“, A. Kapurniotu, R. Kayed, J. W. Taylor, W. Voelter, Eur. J. Biochem., 265, 606-618 (1999).

21. Advanced glycation end products in deposited proteins: detection and reversal“, Y. Al-Abed, A. Kapurniotu, R. Bucala, Methods Enzymol., 309, 152-72 (1999) (Review).

22. „Characterization of catalytic center mutants of macrophage migration inhibitory factor (MIF) and comparison to C81S MIF“, R. Kleemann, A. Kapurniotu, R. Mischke, J. Held, J. Bernhagen, Eur. J. Biochem., 261, 753-766 (1999).

23. „Conformational transitions of islet amyloid polypeptide in amyloid formation in vitro“ R. Kayed, J. Bernhagen, N. Greenfield, K. Sweimeh, H. Brunner, W. Voelter, A. Kapurniotu, J. Mol. Biol., 287, 781-796 (1999).

24. „Model studies of the Maillard reaction of Arg-Lys with D-glucose“, Y.Al-Abed, D. Callaway, A. Kapurniotu, T. Holak, W. Voelter, R. Bucala, Polisch J. Chem., 73, 117-123 (1999).

25. „Specific reduction of insulin disulfides by macrophage migration inhibitory factor (MIF) with glutathione and dihydrolipoamide: potential role in cellular redox processes“, R. Kleemann, R. Mischke, A. Kapurniotu, H. Brunner, J. Bernhagen, FEBS Lett., 430, 191-196 (1998).

26. „Disulfide Analysis Reveals a Role for Macrophage Migration Inhibitory Factor (MIF) as Thiol-protein Oxidoreductase“, R. Kleemann, A. Kapurniotu, R. W. Frank, A. Gessner, R. Mischke, S. Jüttner, H. Brunner, J. Bernhagen., J. Mol. Biol., 280, 85-102 (1998).

27. „Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide (IAPP)“, A. Kapurniotu, J. Bernhagen, N. Greenfield, S. Teichberg, R.W. Frank, Y. Al-Abed, R. Bucala, Eur. J. Biochem., 251, 208-216 (1998).

28. „Structure activity studies of the cytokine macrophage migration inhibitory factor (MIF) reveal a critical role for its carboxy terminus“, R. Mischke, A. Gessner, A. Kapurniotu, S. Jüttner, R. Kleemann, H. Brunner, J. Bernhagen, FEBS Lett., 414, 226-232 (1997).

29. „An agent cleaving glucose-derived protein crosslinks in vitro and in vivo“, S. Vasan, X. Zhang, X. Zhang, A. Kapurniotu, J. Bernhagen, S. Teichberg, J. Basgen, D. Wagle, D. Shih, I. Terlecky, R. Bucala, A. Cerami, J. Egan, P. Ulrich, Nature,  382, 275-278 (1996).

30. „Model studies of the Maillard reaction of Arg-Lys with D-ribose“, Y. Al-Abed, P. Ulrich, A. Kapurniotu, R. Bucala, Bioorganic & Medicinal Chem. Lett., 5, 2929-2930 (1995).

31. „The interaction of (1-4)-fragment of thymosin b4 with calmodulin-sensitive cAMP phospodiesterase from hypothalamus“, W. Voelter, A. Kapurniotu, M. Mihelic, B. Gurvits, G. Abrahamian, A. Galoyan, Neurochem. Res. 20, 55-59 (1995).

32. „Structural and Conformational Requirements for Human Calcitonin Activity: Design, Synthesis and Study of Lactam-Bridged Analogues", A. Kapurniotu & J. W. Taylor, J. Med. Chem., 38, 836-847 (1995).

33. „Head-to-Tail Cyclization and Use of Ca-Allyl Ester Protection Improves the yield of Cyclic Peptides Synthesized by the Oxime Resin Method", A. Kapurniotu & J. W. Taylor, Tetrahedron Letters, 34, 7031-7034 (1993).

34. „Synthesis and two-Dimensional 1H and 13C NMR Investigations of an Inhibitor of Hemato­poietic Stem Cell Proliferation Ac-Ser-Asp-Lys-Pro-OH", J. Freund, A. Kapurniotu, T. A. Holak, M. Lenfant, W. Voelter, Zeitschr. Naturforsch., 47b, 1324-1332 (1992).

35. „Theoretical and experimental epitope mapping of thymosin b4", S. Becker, F.P. Armbruster, B. Müller, H. Echner, A. Kapurniotu, E. Livaniou, M. Mihelic, W. Voelter, J. Immunol. Meth., 177, 131-137 (1994).

36. „Total synthesis of thymosin b4 by fragment condensation", A. Kapurniotu, P. Link, W. Voelter, Liebigs Ann. Chem., 1161-1167 (1993).

37. „Totalsynthese von Thymosin b4, 2. Klassische Synthese des Fragments [20-30] von Thymo­sin b4", A. Kapurniotu & W. Voelter, Liebigs Ann. Chem., 361-370 (1992).

38. „Totalsynthese von Thymosin b4, 1. Klassische Synthese des Fragments [11-19] von Thymo­sin b4", A. Kapurniotu & W. Voelter, Liebigs Ann. Chem., 1251-1257 (1991).



TU München
Helmholz Muenchen
MPI of Neurobiology
MPI of Biochemistry