Interaction analyses of amyloid β peptide (1-40) with glycosaminoglycan model polymers

Yoshiko Miura, Hikaru Mizuno

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

We synthesized a novel glycopolymer library with 6-sulfo-GlcNAc and glucuronicacid(GlcA) based on the structure of glycosaminoglycans. The molecular weights of the polymers were controlled via living radical polymerization. The interactions of Aβ(1-40)ith glycopolymers were analyzed by inhibition activity of protein aggregation using ThT fluorescence assay, atomic force microscopy observation, and CD spectra. The inhibition activity of Aβ was much affected by the sugar structure and molecular weight of the polymer. The glycopolymers carrying 6-sulfo-GlcNAc showed inhibition activity toward Aβ aggregate, and those with 6-suflo-GlcNAc and GlcA showed the strong inhibition activity. The glycopolymer libraries yielded valuable information about Aβ aggregate with glycosaminoglycans.

Original languageEnglish
Pages (from-to)1004-1009
Number of pages6
JournalBulletin of the Chemical Society of Japan
Volume83
Issue number9
DOIs
Publication statusPublished - 2010

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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