Inhibition of Alzheimer amyloid aggregation with sulfated glycopolymers.
Glycopolymers carrying sulfated saccharides with modest sugar contents (11% and 28%) were found to suppress the formation of amyloid fibrils by amyloid beta peptides (Abeta(1-42), Abeta(1-40), and Abeta(25-35)), as evaluated by thioflavin T assays and atomic force microscopy observation. Circular dichroism spectra showed that the conformation of amyloid beta peptides depended on the glycopolymer additives, and that the glycopolymer additives reduced the beta-sheet contents. Neutralization activity was confirmed by in vitro assay with HeLa cells. The sulfate group and the appropriate sugar contents were essential for the inhibitory effect.
Miura
Yoshiko
Y
Department of Molecular Design and Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan. miuray@jaist.ac.jp
Yasuda
Kikuko
K
Yamamoto
Kiyofumi
K
Koike
Mihoko
M
Nishida
Yoshihiro
Y
Kobayashi
Kazukiyo
K
D000682:Amyloid / Q000037:antagonists & inhibitors* / Q000378:metabolism; D002241:Carbohydrates / Q000737:chemistry*; D002942:Circular Dichroism; D018625:Microscopy, Atomic Force; D011108:Polymers / Q000737:chemistry*; D013431:Sulfates / Q000737:chemistry*
D000682:Amyloid; D002241:Carbohydrates; D011108:Polymers; D013431:Sulfates