Inhibition of the amyloid-fibril growth by forming complex between polysaccharide and lysozyme

Mina Sakuragi, Naohiko Shimada, Kazuo Sakurai, Seiji Shinkai

Research output: Contribution to conferencePaper

Abstract

Amyloid-fibril formation causes many incurable diseases and can be characterized to have cross-fiber structures, in which β-strands ally perpendicular to the fiber axis. We have reported that schizophyllan (SPG) can interact with hydrophobic materials. In this study, we demonstrated that SPG interacts with lysozyme formed amyloid fibrils. Circular dichroism (CD) and fluorescence measurements showed that SPG and the amyloid of lysozyme can form a complex having fibrils. Transmission electron micrographs showed that the complex involved short amyloid fibrils compared with native amyloid fibrils. These results indicate that SPG can entrap amyloid fibrils of the lysozyme.

Original languageEnglish
Number of pages1
Publication statusPublished - Oct 19 2006
Event55th SPSJ Annual Meeting - Nagoya, Japan
Duration: May 24 2006May 26 2006

Other

Other55th SPSJ Annual Meeting
CountryJapan
CityNagoya
Period5/24/065/26/06

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All Science Journal Classification (ASJC) codes

  • Engineering(all)

Cite this

Sakuragi, M., Shimada, N., Sakurai, K., & Shinkai, S. (2006). Inhibition of the amyloid-fibril growth by forming complex between polysaccharide and lysozyme. Paper presented at 55th SPSJ Annual Meeting, Nagoya, Japan.