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Morphology Control of Alzheimer Amyloid β Peptide (1-42) on the Multivalent Sulfonated Sugar Interface

Published online by Cambridge University Press:  11 March 2013

Yoshiko Miura  and
Tomohiro Fukuda
Yoshiko Miura
Affiliation:
Department of Chemical Engineering, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan
Tomohiro Fukuda
Affiliation:
Department of Applied Chemistry and Chemical Engineering, Toyama National Collage of Technology, 13 Hogo-machi, Toyama city, Toyama, 939-8630, Japan
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Abstract

The amyloidosis of amyloid β (1-42) was investigated by the well-defined glyco-cluster interface. We prepared monovalent, divalent, and trivalent 6-sulfo-N-acetyl-D-glucosamine immobilized substrates. The interaction between amyloid β and 6-sulfo-N-acetyl-D-glucosamine was amplified by multivalency of divalent and trivalent 6-sulfo-N-acetyl-D-glucosamine. The morphology of amyloid β were investigated by AFM, and we found the morphology of amyloid β aggregates were determined by the kinds of displayed saccharide-valency. Amyloid β had tendency to form spherical objects on the multivalent 6-sulfo-N-acetyl-D-glucosamine, but form fibrils on the monovalent 6-sulfo-N-acetyl-D-glucosamine. Spherical amyloid β was more toxic than fibrillar amyloid β to HeLa cells. These results suggested that the multivalency of was significant in its morphology and aggregation effects at the surface of the cell membrane mimic.

Keywords

biomaterialsurface chemistrycolloid
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1498: Symposium Q – Biomimetic, Bio-inspired and Self-Assembled Materials for Engineered Surfaces and Applications , 2013 , pp. 203 - 206
Copyright
Copyright © Materials Research Society 2013 

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References

REFERENCES

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., Wong, P.C., Neurosci, 25, 11693–11709(2005).CrossRefGoogle Scholar
Selko, D. J., Physiol. Rev., 81, 741–766 (2001).CrossRefGoogle Scholar
Higuchi, M., Iwata, N., Saido, T. C., Biochim. Biophys. Acta., 1751, 60–67(2005).CrossRefGoogle Scholar
Glabe, C.G., J. Biol. Chem. 283, 29639–29643 (2008).CrossRefGoogle Scholar
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Kraft, G. A., Klein, W. L., Proc. Natl. Acad. Sci. USA, 200, 10417–10422 (2003).CrossRefGoogle Scholar
Hoshi, M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., Sato, K., Proc. Natl. Acad. Sci. USA, 100, 6370–6375 (2003).CrossRefGoogle Scholar
McLaurin, J., Franklin, T., Zhang, X., Deng, J., Praser, P. E., Eur. J. Biochem. 266, 1101–1110 (1999).CrossRefGoogle Scholar
Matsuzaki, K., Horikiri, C., Biochemistry, 38, 4137–4142 (1999).CrossRefGoogle Scholar
Fukuda, T., Onogi, S., Miura, Y., Thin Solid Films. 518, 880–888 (2008).CrossRefGoogle Scholar
Chafekar, S. M., Bass, R., Scheper, W., Biochimica. Biophys. Acta. 1782, 523–531 (2008).CrossRefGoogle Scholar