Aggregation of alzheimer amyloid β peptide (1-42) on the multivalent sulfonated sugar interface

Bioconjugate Chemistry

Volumn 21, Issue 6, 2010, Pages 1079-1086

  Fukuda, Tomohiro ^a   Matsumoto, Erino ^a   Onogi, Shunsuke ^a   Miura, Yoshiko ^a  

^a JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; 6 SULFO N ACETYL DEXTRO GLUCOSAMINE; AMYLOID BETA PROTEIN[1-42]; SUGAR; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING AFFINITY; CELL MEMBRANE; CYTOTOXICITY; ELLIPSOMETRY; ENZYME IMMOBILIZATION; ENZYME SUBSTRATE; HELA CELL; HUMAN; HUMAN CELL; MORPHOLOGY; PROTEIN AGGREGATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SENILE PLAQUE; SURFACE PLASMON RESONANCE;

EID: 77953647981     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc100053x     Document Type: Article

References (37)

1. Laird, F. M., Cai, H., Savonenko, A. V., Farah, M. H., He, K., Melnikova, T., Wen, H., Chiang, H.-C., Xu, G., Koliatos, V. E., Borchelt, D. R., Prince, D. L., Lee, H.-K., and Wong, P. C. (2005) BACE1, a major determinant of selective vulnerability of the brain to amyloid-β amyloidogenesis, is essential for cognitive, emotional, and synaptic functions J. Neurosci. 25, 11693-11709
2. Rak, M., Del Bigio, M. R., Mai, S., Westaway, D., and Gough, K. (2007) Dense-core and diffuse Aβ plaques in TgCRND8 mice studied with synchrotron FTIR microspectroscopy Biopolymers 87, 207-217
3. Selkoe, D. J. (2001) Alzheimers disease: Genes, proteins, and therapy Physiol. Rev. 81, 741-766
4. Higuchi, M., Iwata, N., and Saido, T. C. (2005) Understanding molecular mechanisms of proteolysis in Alzheimers disease: Progress toward therapeutic interventions Biochim. Biophys. Acta 1751, 60-67
5. Glabe, C. G. (2008) Structural classification of toxic amyloid oligomers J. Biol. Chem. 283, 29639-29643
6. Okada, T., Ikeda, K., Wakabayashi, M., Ogawa, M., and Matsuzaki, K. (2008) Formation of toxic Aβ(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in Aβ(1-40) fibrils J. Mol. Biol. 382, 1066-1074
7. Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., and Klein, W. L. (2003) Alzheimers disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc. Natl. Acad. Sci. U.S.A. 100, 10417-10422
8. Hoshi, M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., and Sato, K. (2003) Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β Proc. Natl. Acad. Sci. U.S.A. 100, 6370-6375
9. Daggett, V. (2006) α-Sheet: The toxic conformer in amyloid diseases? Acc. Chem. Res. 39, 594-602
10. McLaurin, J., Yang, D. S., Yip, C. M., and Fraser, P. E. (2000) Review: Modulating factors in amyloid-β fibril formation J. Struct. Biol. 130, 259-270
11. Yanagisawa, K. (2007) Role of gangliosides in Alzheimers disease Biochim. Biophys. Acta 1768, 1943-1951
12. McLaurin, J., Franklin, T., Zhang, X., Deng, J., and Fraser, P. E. (1999) Interactions of Alzheimer amyloid-β peptides with glycosaminoglycans: Effects on fibril nucleation and growth Eur. J. Biochem. 266, 1101-1110
13. Matsuzaki, K. and Horikiri, C. (1999) Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes Biochemistry 38, 4137-4142
14. Lee, Y. C. and Lee, R. T. (1995) Carbohydrate-protein interactions: Basis of glycobiology Acc. Chem. Res. 28, 321-327
15. Mammen, M., Choi, S.-K., and Whitesides, G. M. (1998) Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors Angew. Chem., Int. Ed. 37, 2754-2794
16. Mann, D. A., Kanai, M., Maly, D. J., and Kiessling, L. L. (1998) Probing low affinity and multivalent interactions with surface plasmon resonance: Ligands for concanavalin A J. Am. Chem. Soc. 120, 10575-10582
17. Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., and Ihara, Y. (1994) Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43) Neuron 13, 45-53
18. Sasaki, K., Nishida, Y., Kambara, M., Uzawa, H., Takahashi, T., Suzuki, T., Suzuki, Y., and Kobayashi, K. (2004) Design of N -acetyl-6-sulfo-β-D- glucosaminide-based inhibitors of influenza virus sialidase Bioorg. Med. Chem. 12, 1367-1375
19. Miura, Y., Yasuda, K., Yamamoto, K., Koike, M., Nishida, Y., and Kobayashi, K. (2007) Inhibition of Alzheimer amyloid aggregation with sulfated glycopolymers Biomacromolecules 8, 2129-2134
20. Miura, Y. and Mizuno, H. (2009) Interaction of alzheimer amyloid β with glycosaminoglycan model polymer Polym. Prepr., Jpn. 58, 17501
21. Kolb, H. C., Finn, M. G., and Sharpless, K. B. (2001) Click chemistry: Diverse chemical function from a few good reactions Angew. Chem., Int. Ed. 40, 2004-2021
22. Lee, J. K., Chi, Y. S., and Choi, I. S. (2004) Reactivity of acetylenyl-terminated self-assembled monolayers on gold: Triazole formation Langmuir 20, 3844-3847
23. Fukuda, T., Onogi, S., and Miura, Y. (2009) Dendritic sugar-microarrays by click chemistry Thin Solid Films 518, 880-888
24. Matsumoto, E., Yamauchi, T., Fukuda, T., and Miura, Y. (2009) Sugar microarray via click chemistry: Molecular recognition with lectins and amyloid β (1-42) Sci. Technol. Adv. Mater. 10 034605
25. Miura, Y., Yamauchi, T., Sato., H., and Fukuda, T. (2008) The self-assembled monolayer of saccharide via click chemistry: Formation and protein recognition Thin Solid Films 516, 2443-2449
26. Hoos, M. D., Ahmed, M., Smith, S. O., and Van Nostrand, W. E. (2009) Myelin basic protein binds to and inhibits the fibrillar assembly of Aβ42 in vitro Biochemistry 48, 4720-4727
27. Schmechel, A., Zentgraf, H., Scheuermann, S., Fritz, G., Pipkorn, R., Reed, J., Beyreuther, K., Bayer, T. A., and Multhaup, G. (2003) Alzheimer β-amyloid homodimers facilitate Aβ fibrillization and the generation of conformational antibodies J. Biol. Chem. 278, 35317-35324
28. Ban., T., Morigaki, K., Yagi, H., Kawasaki, T., Kobayashi, A., Yuba, S., Naiki, H., and Goto, Y. (2006) Real-time and single fibril observation of the formation of amyloid β spherulitic structures J. Biol. Chem. 281, 33677-33683
29. Hiramatsu, H., Goto, Y., Naiki, H., and Kitagawa, T. (2004) Core structure of amyloid fibril proposed from IR-microscope linear dichroism J. Am. Chem. Soc. 126, 3008-3009
30. Zurdo, J., Guijarro, J. I., and Dobson, C. M. (2001) Preparation and characterization of purified amyloid fibrils J. Am. Chem. Soc. 123, 8141-8142
31. Ingemarson, R. and Thelander, L. (1996) A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase Biochemistry 35, 8603-8609
32. Ulman, A. (1996) Formation and structure of self-assembled monolayers Chem. Rev. 96, 1533-1554
33. Giulian, D., Haverkamp, L. J., Yu, J., Karshin, W., Tom, D., Li, J., Kazanskaia, A., Kirkpatrick, J., and Roher, A. E. (1998) The HHQK domain of β-amyloid provides a structural basis for the immunopathology of Alzheimers disease J. Biol. Chem. 273, 29719-29726
34. Takahashi, T. and Mihara, H. (2008) Peptide and protein mimetics inhibiting amyloid β-peptide aggregation Acc. Chem. Res. 41, 1309-1318
35. Schneider, J. P. and Kelly, J. W. (1995) Templates that induce α-helical, β-sheet, and loop conformations Chem. Rev. 95, 2169-2187
36. Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, E. C., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., Wals, P., Zhang, C., Finch, C. E., Krafft, G. A., and Klein, W. L. (1998) Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins Proc. Natl. Acad. Sci. U.S.A. 95, 6448-6453
37. Zako, T., Sakono, M., Hashimoto, N., Ihara, M., and Maeda, M. (2009) Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils Biophys. J. 96, 3331-3340