Fullerene inhibits β-amyloid peptide aggregation

Biochemical and Biophysical Research Communications

Volumn 303, Issue 2, 2003, Pages 576-579

  Kim, Jeong Eun ^a   Lee, Minyung ^a  

^a Ewha Womans University   (South Korea)

Author keywords

Aggregation; Alzheimer; Amyolid; Fluorescence; Fullerene; Hydrophobicity; Inhibitor; Melatonin; Oligomer; Thioflavin T

Indexed keywords

2,4 DINITROPHENOL; AMYLOID BETA PROTEIN; BENZOFURAN DERIVATIVE; BENZOQUINONE; DAUNORUBICIN; FULLERENE; MELATONIN; PROTEIN INHIBITOR; ROLITETRACYCLINE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DRUG EFFECT; DRUG PROTEIN BINDING; IC 50; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN MOTIF;

EID: 0037418703     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00393-0     Document Type: Article

References (34)

1. Hardy J., Higgins G.A. The amyloid cascade hypothesis. Science. 256:1992;184-185.
2. Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 297:2000;353-356.
3. See, for example, R. Wetzel (Ed.), Amyloid, Prions, and Other Protein Aggregates, Methods in Enzymology, vol. 309, 1999.
4. Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA. 93:1996;1125-1129.
5. 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.
6. Esler W.P., Stimson E.R., Jennings J.M., Vinters H.V., Ghilardi J.R., Lee J.P., Mantyh P.W., Maggio J.E. Deposition of monomeric, not oligomeric, Aβ mediates growth of Alzheimer's disease amyloid plagues in human brain preparations. Biochemistry. 39:2000;6288-6295.
7. Pallitto M.M., Murphy R.M. A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state. Biophys. J. 81:2001;1805-1822.
8. 1-42 are potent central nervous system neurotoxins Proc. Natl. Acad. Sci. USA. 95:1998;6448-6453.
9. Hafner J.H., Cheung C.L., Woolley A.T., Lieber C.M. Structural and functional imaging with carbon nanotube AFM probes. Prog. Biophys. Mol. Biol. 77:2001;73-110.
10. Lue L.F.et al. Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. pathol. 155:1999;853-862.
11. 1-42 in wild type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation J. Neurosci. 20:2000;4050-4058.
12. Klein W.L., Krafft G.A., Finch C.E. Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24:2001;219-224.
13. Hilbich C., Kisters-woike B., Reed J., Masters C.L., Beyreuther K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease βA4 peptides. J. Mol. Biol. 218:1991;149-163.
14. Burdick D., Soreghan B., Kwon M., Kosmoski J., Knauer M., Henschen A., Yates J.J., Cotman C., Glabe C. Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J. Biol. Chem. 267:1992;546-554.
15. Tjernberg L.O., Naslund J., Lindqvist F., Johansson J., Karlstrom R., Thyberg J., Terenius L., Nordstedt C. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 271:1996;8545-8548.
16. Tjernberg L.O., Callaway J.E., Tjernberg A., Hahne S., Lilliehook C., Terenius L., Thyberg J., Nordstedt C. A molecular model of Alzheimer amyloid β-peptide fibril formation. J. Biol. Chem. 274:1999;12619-12625.
17. 16-22, a a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR Biochemistry. 39:2000;13748-13759.
18. Findeis M.A. Approaches to discovery and characterization of inhibitors of amyloid β-peptide polymerization. Biochim. Biophys. Acta. 1502:2000;76-84.
19. Lowe T.L., Strzelec A., Kiessling L.L., Murphy R.M. Structure-function relationships for inhibitors of β-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry. 40:2001;7882-7889.
20. Fassbender K., Masters C., Beyreuther K. Alzheimer's disease: molecular concepts and therapeutic targets. Naturwissenschaften. 88:2001;261-267.
21. Lashuel H.A., Hartley D.M., Balakhaneh D., Aggarwal A., Teichberg S., Callaway J.E. New class of inhibitors of amyloid-β fibril formation. J. Biol. Chem. 45:2002;42881-42890.
22. Dugan L.L.et al. Carboxyfullerenes as neuroprotective agents. Proc. Natl. Acad. Sci. USA. 94:1997;9434-9439.
23. Huang Y.L., Shen C.K., Luh T.Y., Yang H.C., Hwang K.C., Chou C.K. Blockage of apoptotic signaling of transforming growth factor-β in human hepatoma cells by carboxyfullerene. Eur. J. Biochem. 254:1998;38-43.
24. Chen B.X., Wilson S.R., Das M., Coughlin D.J., Erlanger B.F. Antigenicity of fullerenes: antibodies specific for fullerenes and their characteristics. Proc. Natl. Acad. Sci. USA. 95:1998;10809-10813.
25. 60 carboxyfullerene exerts a protective activity against oxidative stress-induced apoptosis in human peripheral blood mononuclear cells Biochem. Biophys. Res. Commun. 277:2000;711-717.
26. 60 J. Phys. Chem. 105:2001;2499-2506.
27. LeVine H. III Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;404-410.
28. Howlett D.R., Perry A.E., Godfrey F., Swatton J.E., Jennings K.H., Spitzfaden C., Wadsworth H., Wood S.J., Markwell R.E. Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans. Biochem. J. 340:1999;283-289.
29. ′ -(3-diethylaminopropoxy)-phenyl]-benzofuran do not act as surfactants or micelles when inhibiting the aggregation of β-amyloid peptide Bioorg. Med. Chem. Lett. 11:2001;255-257.
30. Howlett D.R., George A.R., Owen D.E., Ward R.V., Markwell R.E. Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation. Biochem. J. 343:1999;419.
31. Felice F.G.et al. Inhibition of Alzheimer's disease β-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy. FASEB J. 15:2001;1297-2000.
32. Wood S.J., MacKenizies L., Maleeff B., Hurle M.R., Wetzel R. Selective inhibition of Aβ fibril formation. J. Biol. Chem. 271:1996;4086.
33. Poeggeler B.et al. Melatonin reverses the profibrillogenic activity of apoliporprotein E4 on the Alzheimer amyloid Aβ peptide. Biochemistry. 40:2001;14995-15001.
34. Skribanek Z., Balaspiri L., Mak M. Interaction between synthetic amyloid-β-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry. J. Mass Spectrom. 36:2001;1226-1229.