Inhibition of hIAPP amyloid-fibril formation and apoptotic cell death by a designed hIAPP amyloid-core-containing hexapeptide

Chemistry and Biology

Volumn 12, Issue 7, 2005, Pages 797-809

  Tatarek Nossol, Marianna ^a   Yan, Li Mei ^a   Schmauder, Anke ^a   Tenidis, Konstantinos ^a   Westermark, Gunilla ^b   Kapurniotu, Aphrodite ^a  

^a RWTH AACHEN UNIVERSITY   (Germany)

^b LINKÖPING UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; ISLET AMYLOID POLYPEPTIDE (8 37); ISLET AMYLOID POLYPEPTIDE (8-37); OLIGOPEPTIDE; PEPTIDE FRAGMENT;

AMYLOIDOSIS; ARTICLE; CELL CULTURE; CELL DEATH; CELL SURVIVAL; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; METABOLISM; METHYLATION; SPECTROFLUOROMETRY;

AMYLOID; AMYLOIDOSIS; CELL DEATH; CELL SURVIVAL; CELLS, CULTURED; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; METHYLATION; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; SPECTROMETRY, FLUORESCENCE;

EID: 22544474421     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2005.05.010     Document Type: Article

References (68)

1. R.L. Hull, G.T. Westermark, P. Westermark, and S.E. Kahn Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes J. Clin. Endocrinol. Metab. 89 2004 3629 3643
2. S. Ahmed, A. Clark, and D.R. Matthews Progressive decline of β-cell function in non-insulin dependent diabetes Curr. Opin. Endocrinol. Diabetes 4 1997 300 307
3. E.L. Opie On the relation of chronic interstitial pancreatitis to the islands of Langerhans and to diabetes mellitus J. Exp. Med. 5 1901 397 428
4. P. Westermark, C. Wernstedt, E. Wilander, D.W. Hayden, T.D. O'Brien, and K.H. Johnson Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells Proc. Natl. Acad. Sci. USA 84 1987 3881 3885
5. S.J. Wimalawansa Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin: a peptide superfamily Crit. Rev. Neurobiol. 11 1997 167 239
6. B. Nyholm, M.S. Finernan, J.E. Koda, and O. Schmitz Plasma amylin immunoreactivtiy and insulin resistance in insulin resistant relatives of patients with non-insulin-dependent diabetes mellitus Horm. Metab. Res. 30 1998 206 212
7. A. Lorenzo, B. Razzboni, G.C. Weir, and B.A. Yankner Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus Nature 368 1994 756 760
8. A. Kapurniotu Amyloidogenicity and cytotoxicity of islet amyloid polypeptide Biopolymers 60 2001 438 459
9. J. Janson, R.H. Ashley, D. Harrison, S. McIntyre, and P.C. Butler The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles Diabetes 48 1999 491 498
10. M. Anguiano, R. Nowak, and P.T.J. Lansbury Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes Biochemistry 41 2002 11338 11343
11. Y. Porat, S. Kolusheva, R. Jelinek, and E. Gazit The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies Biochemistry 42 2003 10971 10977
12. J.D. Green, C. Goldsbury, J. Kistler, G.J. Cooper, and U. Aebi Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation J. Biol. Chem. 279 2004 12206 12212
13. R. Kayed, J. Bernhagen, N. Greenfield, K. Sweimeh, H. Brunner, W. Voelter, and A. Kapurniotu Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro J. Mol. Biol. 287 1999 781 796
14. S.B. Padrick, and A.D. Miranker Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis Biochemistry 41 2002 4694 4703
15. A. Lorenzo, and B.A. Yankner β-amyloid neurotoxicity requires fibril formation and is inhibited by congo red Proc. Natl. Acad. Sci. USA 91 1994 12243 12247
16. T. Tomiyama, H. Kaneko, K. Kataoka, S. Asano, and N. Endo Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction Biochem. J. 322 1997 859 865
17. Y.C. Kudva, C. Mueske, P.C. Butler, and N.L. Eberhardt A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation Biochem. J. 331 1998 809 813
18. J.F. Aitken, K.M. Loomes, B. Konarkowska, and G.J.S. Cooper Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid Biochem. J. 374 2003 779 784
19. T.A. Harroun, J.P. Bradshaw, and R.H. Ashley Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation FEBS Lett. 507 2001 200 204
20. L.A. Scrocchi, Y. Chen, S. Waschuk, F. Wang, S. Cheung, A.A. Darabie, J. McLaurin, and P.E. Fraser Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis J. Mol. Biol. 318 2002 697 706
21. S. Gilead, and E. Gazit Inhibition of amyloid formation by peptide analogues modified with α-aminoisobutyric acid Angew. Chem. Int. Ed. Engl. 43 2004 4041 4044
22. A. Kapurniotu, A. Schmauder, and K. Tenidis Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity J. Mol. Biol. 315 2002 339 350
23. K. Rajarathnam, I. Clark-Lewis, and B.D. Sykes 1H NMR solution structure of an active monomeric interleukin-8 Biochemistry 34 1995 12983 12990
24. X. Sun, and G.P. Lorenzi On the stacking of β-rings: the solution self-association behavior of two partially N-methylated cyclo(hexaleucines) Helv. Chim. Acta 77 1994 1520 1526
25. P. Chitnumsub, W.R. Fiori, H.A. Lashuel, H. Diaz, and J.W. Kelly The nucleation of monomeric parallel β-sheet-like structures and their self-assambly in aqueous solution Bioorg. Med. Chem. 7 1999 39 59
26. S. Sagan, P. Karoyan, O. Lequin, G. Chassaing, and S. Laviell N- and Cα-methylation in biologically active peptides: synthesis, structural and functional aspects Curr. Med. Chem. 11 2004 2799 2822
27. D.J. Gordon, K.L. Sciarretta, and S.C. Meredith Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid congeners containing N-methyl amino acids at alternate residues Biochemistry 40 2001 8237 8245
28. E. Hughes, R.M. Burke, and A.J. Doig Inhibition of toxicity in the β-amyloid peptide fragment β-(25-35) using N-methylated derivatives J. Biol. Chem. 275 2000 25109 25115
29. K. Tenidis, M. Waldner, J. Bernhagen, W. Fischle, M. Bergmann, M. Weber, M.-L. Merkle, W. Voelter, H. Brunner, and A. Kapurniotu Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties J. Mol. Biol. 295 2000 1055 1071
30. D. Zanuy, B. Ma, and R. Nussinov Short peptide amyloid organization: stabilities and conformations of the islet amyloid polypeptide NFGAIL Biophys. J. 84 2003 1884 1894
31. D. Zanuy, Y. Porat, E. Gazit, and R. Nussinov Peptide sequence and amyloid formation; molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs Structure 12 2004 439 455
32. J.M. Griffiths, T.T. Ashburn, M. Auger, P. Costa, R.G. Griffin, and P.T.J. Lansbury Rotational resonance solid-state NMR elucidates a structural model of pancreatic amyloid J. Am. Chem. Soc. 117 1995 3539 3546
33. A. Kapurniotu, J. Bernhagen, N. Greenfield, Y. Al-Abed, S. Teichberg, R.W. Frank, W. Voelter, and R. Bucala Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide Eur. J. Biochem. 251 1998 208 216
34. J.T. Jarrett, and P.T. Lansbury Jr. Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058
35. R.W. Woody Circular dichroism of peptides S. Udenfriend J. Meienhofer V. Hruby The Peptides: Analysis, Synthesis, Biology 1985 Academic Press New York 15 114
36. C. Goldsbury, K. Goldie, J. Pellaud, J. Seelig, P. Frey, S.A. Müller, J. Kistler, G.J.S. Cooper, and U. Aebi Amyloid fibril formation from full-length and fragments of amylin J. Struct. Biol. 130 2000 352 362
37. D.F. Moriarty, and D.P. Raleigh Effects of sequential proline substitutions on amyloid formation by human amylin20-29 Biochemistry 38 1999 1811 1818
38. P. Westermark, U. Engström, K. Johnson, G.T. Westermark, and C. Betsholz Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation Proc. Natl. Acad. Sci. USA 87 1990 5036 5040
39. H. LeVine 3rd. Quantification of β-sheet amyloid fibril structures with thioflavin T R. Wetzel Methods in Enzymology: Amyloid, Prions, and Other Protein Aggregates 1999 Academic Press New York 274 284
40. H. LeVine 3rd. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution Protein Sci. 2 1993 404 410
41. S.B. Padrick, and A.D. Miranker Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway J. Mol. Biol. 308 2001 783 794
42. M.S. Shearman, S.R. Hawtin, and V.J. Tailor The intracellular component of cellular 3-(4,5-dimethythiazol-2-yl)-2,5-Diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides J. Neurochem. 65 1995 218 227
43. M.S. Shearman, C.I. Ragan, and L.L. Iversen Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death Proc. Natl. Acad. Sci. USA 91 1994 1470 1474
44. D. Schubert, C. Behl, R. Lesley, A. Brack, R. Dargusch, Y. Sagara, and H. Kimura Amyloid peptides are toxic via a common oxidative mechanism Proc. Natl. Acad. Sci. USA 92 1995 1989 1993
45. A. Kapurniotu, A. Buck, M. Weber, A. Schmauder, T. Hirsch, J. Bernhagen, and M. Tatarek-Nossol Conformational restriction via cyclization in β-amyloid peptide Aβ(1-28) leads to an inhibitor of Aβ(1-28) amyloidogenesis and cytotoxicity Chem. Biol. 10 2003 149 159
46. E.L. Saafi, B. Konarkowska, S. Zhang, J. Kistler, and G. Cooper Ultrastructural evidence that apoptosis is the mechanism by which human amylin evokes death in RINm5F pancreatic beta-cells Cell Biol. Int. 25 2001 339 350
47. S. Zhang, J. Liu, G. MacGibbon, M. Dragunow, and G.J.S. Cooper Increased expression and activation of c-Jun contributes to human amylin induced apoptosis in pancreatic islet β-cells J. Mol. Biol. 324 2002 271 285
48. R.C. Duke, and J.J. Cohen IL-2 addiction: withdrawal of growth factor activates a suicide program in dependent T cells Lymphokine Res. 5 1986 289 299
49. A. Corsaro, S. Thellung, V. Villa, D.R. Principe, D. Paludi, S. Arena, E. Millo, D. Schettini, G. Damonte, and A. Aceto Prion protein fragment 106-126 induces a p38 MAP kinase-dependent apoptosis in SH-SY5Y neuroblastoma cells independently from the amyloid fibril formation Ann. N Y Acad. Sci. 1010 2003 610 622
50. H. Puchtler, and F. Sweat Congo red as a stain for fluorescence microscopy of amyloid J. Histochem. Cytochem. 13 1965 693 694
51. J.H. Cooper Selective amyloid staining as a function of amyloid composition and structure Lab. Invest. 31 1974 232 238
52. E. Gazit Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: implications for the design of fibrillization inhibitors Curr. Med. Chem. 9 2002 1725 1735
53. Y. Mazor, S. Gilead, I. Benhar, and E. Gazit Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide J. Mol. Biol. 322 2002 1013 1024
54. R. Azriel, and E. Gazit Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide J. Biol. Chem. 276 2001 34156 34161
55. M.C. Manning, M. Illangasekare, and R.W. Woody Circular dichroism studies of distorted α-helices, twisted β-sheets, and β-turns Biophys. Chem. 31 1988 77 86
56. D.J. Gordon, R. Tappe, and S.C. Meredith Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Ab1-40 fibrillogenesis J. Pept. Res. 2002 2002 37 55
57. H. LeVine 3rd, and J.D. Scholten Screening for pharmacological inhibitors of amyloid fibril formation R. Wetzel Methods of Enzymology: Amyloid, Prions, and Other Protein Aggregates 1999 Academic Press New York 467 476
58. M.R. Eftink Fluorescence methods for studying equilibrium macromolecule-ligand interactions L. Brand M.L. Johnson Methods in Enzymology: Fluorescence Spectroscopy 1997 Academic Press New York 221 257
59. L.O. Tjerberg, A. Pramanik, S. Björling, P. Thyberg, J. Thyberg, C. Nordstedt, K.D. Berndt, L. Terenious, and R. Rigler Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy Chem. Biol. 6 1999 53 62
60. R.G. Maroun, S. Gayet, M.S. Benleulmi, H. Porumb, L. Zargarian, H. Merad, H. Leh, J.F. Mouscadet, F. Troalen, and S. Fermandjian Peptide inhibitors of HIV-1 integrase dissociate the enzyme oligomers Biochemistry 40 2001 13840 13848
61. T.A. Mirzabekov, M. Lin, and B.L. Kagan Pore formation by the cytotoxic islet amyloid peptide amylin J. Biol. Chem. 271 1996 1988 1992
62. C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. Suppl. 10 2004 10 17
63. T. Tomiyama, A. Shoji, K. Kataoka, Y. Suwa, S. Asano, H. Kaneko, and N. Endo Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin J. Biol. Chem. 271 1996 6839 6844
64. G.T. Westermark, K.H. Johnson, and P. Westermark Staining methods for identification of amyloid in tissue R. Wetzel Methods in Enzymology: Amyloid, Prions, and Other Protein Aggregates 1999 Academic Press New York 3 25
65. C. Adessi, M.J. Frossard, C. Boissard, S. Fraga, S. Bieler, T. Ruckle, F. Vilbois, S.M. Robinson, M. Mutter, and W.A. Banks Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease J. Biol. Chem. 278 2003 13905 13911
66. K. Wiesehan, K. Buder, R.P. Linke, S. Patt, M. Stoldt, E. Unger, B. Schmitt, E. Bucci, and D. Willbold Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display ChemBioChem 4 2003 748 753
67. A. Kapurniotu, R. Kayed, J.W. Taylor, and W. Voelter Rational design, confomational studies and bioactivity of novel, highly potent, conformationally constrained calcitonin analogues Eur. J. Biochem. 265 1999 606 618
68. W.A. Lim, R.O. Fox, and F.M. Richards Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5 Protein Sci. 3 1994 1261 1266