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

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.