Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro

Journal of Molecular Biology

Volumn 287, Issue 4, 1999, Pages 781-796

  Kayed, Rakez ^a   Bernhagen, Jürgen ^b   Greenfield, Norma ^c   Sweimeh, Khuloud ^a   Brunner, Herwig ^b   Voelter, Wolfgang ^a   Kapurniotu, Aphrodite ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b UNIVERSITY OF STUTTGART   (Germany)

^c RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

Amyloid; Circular dichroism; Islet amyloid polypeptide (IAPP); Nucleation dependence; Partially folded state

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLIN; AMYLOID; GLOBULAR PROTEIN;

ALZHEIMER DISEASE; AMYLOIDOSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; BIOCHEMISTRY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ELECTRON MICROSCOPY; HUMAN; HYDROPHOBICITY; NON INSULIN DEPENDENT DIABETES MELLITUS; PANCREAS DISEASE; POLARIMETRY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUBILIZATION; TEMPERATURE; ULTRAVIOLET SPECTROSCOPY;

EID: 0033538015     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2646     Document Type: Article

References (63)

1. Ashburn T. T., Lansbury P. T. Jr. Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation: peptide models of pancreatic amyloid. J. Am. Chem. Soc. 115:1993;11012-11013.
2. Ashburn T. T., Auger M., Lansbury P. T. Jr. The structural basis of pancreatic amyloid formation: isotope-edited spectroscopy in the solid state. J. Am. Chem. Soc. 114:1992;790-791.
3. Barrow C. J., Zagorski M. G. Solution structure of β-peptide and its constituent fragments: relation to amyloid deposition. Science. 253:1991;179-182.
4. Booth D. R., Sunde M., Bellotti V., Robinson C. V., Hutchinson W. L., Fraser P. E., Hawkins P. N., Dobson C. M., Radford S. E., Blake C. C. F., Pepys M. B. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 385:1997;787-793.
5. Brahms S., Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138:1980;149-178.
6. Brems D. N., Plaisted S. M., Kauffman E. W., Havel H. A. Characterization of an associated equilibrium folding intermediate of bovine growth hormone. Biochemistry. 25:1986;6539-6543.
7. Chargé S., de Koning E. J. P., Clark A. Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro. Biochemistry. 34:1995;14588-14593.
8. Clark A., Cooper G. J. S., Lewis S. E. Islet amyloid formed from diabetes associated peptide may be pathogenic in type-2 diabetes. Lancet. ii:1987;231-234.
9. Come J. H., Fraser P. E., Lansbury P. T. Jr. A kinetic model for amyloid formation in the prion diseases: Importance of seeding. Proc. Natl Acad. Sci. USA. 90:1993;5959-5963.
10. Cooper G. J. S., Willis A. C., Clark A., Turner R. C., Sim R. B., Reid K. B. M. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl Acad. Sci. USA. 84:1987;8628-8632.
11. Cooper G. J. S., Leighton B., Dimitriadis G. D., Parry-Billings M., Kowalchuck J. M., Howland K., Rothbard J. B., Willis A. C., Reid K. B. M. Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in sceletal muscle. Proc. Natl Acad. Sci. USA. 85:1988;7763-7766.
12. Cort J., Liu Z., Harris S. M., Prickett K. S. M., Gaeta L. S. L., Andersen N. H. β structure in human amylin and two designer β-peptides: CD and NMR spectroscopic comparisons suggest soluble β-oligomers and the absence of significant populations of β-strand dimers. Biochem. Biophys. Res. Commun. 204:1994;1088-1095.
13. De Young L. R., Fink A. L., Dill K. A. Aggregation of globular proteins. Acc. Chem. Res. 25:1993a;614-620.
14. De Young L. R., Dill K., Fink A. L. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry. 32:1993b;3877-3886.
15. Goldsbury C. S., Cooper G. J. S., Goldie K. N., Müller S. A., Saafi E. L., Gruijters W. T. M., Misur M. P., Engel A., Aebi U., Kistler J. Polymorphic fibrillar assembly of human amylin. J. Struct. Biol. 119:1997;17-27.
16. Greenfield N. J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 235:1996;1-10.
17. Griffiths J. M., Ashburn T. T., Auger M., Costa P. R., Griffin R. G., Lansbury P. T. Jr. Rotational resonance solid-state NMR elucidates a structural model of pancreatic amyloid. J. Am. Chem. Soc. 117:1995;3539-3546.
18. Guijarro J. I., Sunde M., Jones J. A., Campbell I. D., Dobson C. M. Amyloid fibril formation by an SH3 domain. Proc. Natl Acad. Sci. USA. 95:1998;4224-4228.
19. Harper J. D., Lansbury P. T. Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407.
20. Harper J. D., Lieber C. M., Lansbury P. T. Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β-protein. Chem. Biol. 4:1997;951-959.
21. Hilbich C., Kisters-Woike B., Reed J., Masters C. L., Beyreuther K. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 218:1991;149-163.
22. Hirota N., Mizuno K., Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275:1998;365-378.
23. Jaenicke R., Rudolph R. Refolding and association of oligomeric proteins. Methods Enzymol. 131:1986;218-250.
24. Jarrett J. T., Lansbury P. T. Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73:1993;1055-1058.
25. Kapurniotu A., Bernhagen J., Greenfield N., Al-Abed Y., Teichberg S., Frank R., Voelter W., Bucala R. Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide (IAPP). Eur. J. Biochem. 251:1998;208-216.
26. Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
27. Kominos D. Towards understanding amyloid aggregation. Biophys. J. 69:1995;739-740.
28. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103.
29. Lai Z., Colon W., Kelly J. W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry. 35:1996;6470-6482.
30. Lansbury P. T. Jr. In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information. Biochemistry. 31:1992;6865-6870.
31. Lansbury P. T. Jr, Caughey B. The chemistry of scrapie infection: implications of the 'ice 9' methaphor. Chem. Biol. 2:1995;1-5.
32. Litvinovich S. V., Brew S. A., Aota S., Akiyama S. K., Haudenschild C., Ingham K. C. Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280:1998;245-258.
33. Lorenzo A., Yankner B. A. β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl Acad. Sci. USA. 91:1994;12243-12247.
34. Lorenzo A., Razzoboni B., Weir G. C., Yankner B. A. Pancreatic islet toxicity of amylin associated with type-2 diabetes mellitus. Nature. 368:1994;756-760.
35. Lu H., Buck M., Radford S. E., Dobson C. M. Acceleration of the folding of hen lysozyme by trifluoroethanol. J. Mol. Biol. 265:1997;112-117.
36. Maeda H. Irreversible nature of the stacked β-pleated sheets of a model polypeptide. Bull. Chem. Soc. Jpn. 60:1987;3438-3440.
37. Maeda H., Ooi K. Isodichroic point and the xβ-random coil transition of poly(S-carboxymethyl- L -cystein) and poly(S-carboxyethyl- L -cysteine) in the absence of added salt. Biopolymers. 20:1981;1549-1563.
38. Naiki H., Nakakuki K. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab. Invest. 74:1996;374-383.
39. Pan K. M., Baldwin M., Nguyen N., Gasset M., Serban A., Groth D., Mehlhom I., Huang Z., Fletterick R. J., Cohen F. E. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA. 90:1993;10962-10966.
40. Perczel A., Park K., Fasman G. D. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide. Anal. Biochem. 203:1992;83-93.
41. Pike C. J., Walencewicz A. J., Glabe C. G., Cotman C. W. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563:1991;311-314.
42. Ptitsyn O. B. Molten globule and protein folding. Advan. Protein. Chem. 47:1995;83-229.
43. Safar J., Roller P. P., Carleton Gajdusek D., Gibbs C. J. Jr. Scrapie amyloid prion protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry. 33:1994;8375-8383.
44. Saldanha J., Mahadevan D. Molecular model-building of amylin and calcitonin gene-related polypeptide hormones using a combination of knowledge sources. Protein Eng. 4:1991;539-544.
45. Saito K., Maeda H., Ikeda S. Reversible and irreversible conversion between the intermolecular β-structure and the disordered state of poly(S-carboxymethyl- L -cysteine) in aqueous media. Biophys. Chem. 16:1982;67-77.
46. Schönbrunner N., Wey J., Engels J., Georg H., Kiefhaber T. Native-like-structure in a trifluorethanol-induced partially folded state of the all-β-sheet protein tendamistat. J. Mol. Biol. 260:1996;432-445.
47. Semisotnov G. V., Rodionova N. A., Razgulyaev O. I., Uversky V. N., Gripas A. F., Gilmanshin R. I. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31:1991;119-128.
48. Shen C.-L., Murphy R. M. Solvent effects on self-assembly of β-amyloid peptide. Biophys. J. 69:1995;640-651.
49. Sipe J. D. Amyloidosis. Crit. Rev. Clin. Lab. Sci. 31:1994;324-354.
50. Soto C., Frangione B. Two conformational states of amyloid β-peptide: implications for the pathogenesis of Alzheimer's disease. Neurosci. Letters. 186:1995;115-118.
51. Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:1965;482-495.
52. Swietnicki W., Petersen R., Gambetti P., Surewicz W. K. . pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272:1997;27517-27520.
53. Terzi E., Hölzemann G., Seelig J. Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35). Biochemistry. 33:1994;1345-1350.
54. Thomas P. J., Qu B.-H., Pedersen P. L. Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20:1995;456-459.
55. Tilstra L., Mattice W. L. The β-sheet-coil transition of polypeptides, as determined by circular dichroism. Fasman G. D. Circular Dichroism and the Conformational Analysis of Biomolecules. 1997;261-284 Plenum Press, New York and London.
56. Urry D. W., Luan C. H., Parker T. M., Gowda D. C., Prasad K. U., Reid M. C., Safavy A. Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity. J. Am. Chem. Soc. 113:1991;4346-4348.
57. Weinreb P. H., Jarrett J. T., Lansbury P. T. Jr. Peptide models of a hydrophobic cluster at the C-terminus of the β-amyloid protein. J. Am. Chem. Soc. 116:1994;10835-10836.
58. Westermark P., Wernstedt C., Wilander E., Hayden D. W., O'Brien T. D., Johnson K. H. 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.
59. Westermark P., Engström U., Johnson K., Westermark G. T., Betsholz C. Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation. Proc. Natl Acad. Sci. USA. 87:1990;5036-5040.
60. Wetzel R. For protein misassembly it's the "I" decade. Cell. 86:1996;699-702.
61. Wood S. J., Maleeff B., Hart T., Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ J. Mol. Biol. 256:1996;870-877.
62. Woody R. W., Dunker K. Aromatic and cystine side-chain circular dichroism in proteins. Fasman G. D. Circular Dichroism and the Conformational Analysis of Biomolecules. 1997;109-158 Plenum Press, New York and London.
63. Yang J. T., Wu C-S. C., Martinez H. M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1986;208-269.