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

Yoshiko Miura, Tomohiro Fukuda

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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 multivalentcy 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.

Original languageEnglish
Title of host publicationBiomimetic, Bio-Inspired and Self-Assembled Materials for Engineered Surfaces and Applications
Pages203-206
Number of pages4
DOIs
Publication statusPublished - 2013
Event2012 MRS Fall Meeting - Boston, MA, United States
Duration: Nov 25 2012Nov 30 2012

Publication series

NameMaterials Research Society Symposium Proceedings
Volume1498
ISSN (Print)0272-9172

Other

Other2012 MRS Fall Meeting
CountryUnited States
CityBoston, MA
Period11/25/1211/30/12

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials
  • Mechanical Engineering

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